Abstract

The temperature-sensitive gating of human Connexin 26 (hCx26) was analyzed with confocal Raman microscopy. High-resolution Raman spectra covering the spectral range between 400 and 1500 rel. cm−1 with a spectral resolution of 1 cm−1 were fully annotated, revealing notable differences between the spectrum recorded from solubilized hCx26 in Ca2+-buffered POPC at 10°C and any other set of protein conditions (temperature, Ca2+ presence, POPC presence). Spectral components originating from specific amino acids show that the TM1/EL1 parahelix and probably the TM4 trans-membrane helix and the plug domain are involved in the gating process responsible for fully closing the hemichannel.

© 2014 Optical Society of America

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    [CrossRef] [PubMed]
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    [CrossRef] [PubMed]

2013 (3)

A. Rygula, K. Majzner, K. M. Marzec, A. Kaczor, M. Pilarczyk, and M. Baranska, “Raman spectroscopy of proteins: a review,” J. Raman Spectrosc.44(8), 1061–1076 (2013).
[CrossRef]

G. P. Sousa, P. T. C. Freire, J. Mendes Filho, F. E. A. Melo, and C. L. Lima, “Low-Temperature Raman Spectra of L-Histidine Crystals,” Braz. J. Phys.43(3), 137–144 (2013).
[CrossRef]

F. Zonta, G. Polles, M. F. Sanasi, M. Bortolozzi, and F. Mammano, “The 3.5 ångström X-ray structure of the human connexin26 gap junction channel is unlikely that of a fully open channel,” Cell Commun. Signal.11(1), 15 (2013), http://www.biosignaling.com/content/pdf/1478-811X-11-15.pdf .
[CrossRef] [PubMed]

2012 (4)

T. Kwon, B. Roux, S. Jo, J. B. Klauda, A. L. Harris, and T. A. Bargiello, “Molecular dynamics simulations of the Cx26 hemichannel: insights into voltage-dependent loop-gating,” Biophys. J.102(6), 1341–1351 (2012).
[CrossRef] [PubMed]

F. Zonta, G. Polles, G. Zanotti, and F. Mammano, “Permeation pathway of homomeric connexin 26 and connexin 30 channels investigated by molecular dynamics,” J. Biomol. Struct. Dyn.29(5), 985–998 (2012).
[CrossRef] [PubMed]

J. Jehlička, A. Oren, and H. G. M. Edwards, “Raman spectra of osmotic solutes of halophiles,” J. Raman Spectrosc.43(8), 1134–1140 (2012).
[CrossRef]

T. A. Bargiello, Q. Tang, S. Oh, and T. Kwon, “Voltage-dependent conformational changes in connexin channels,” Biochim. Biophys. Acta1818(8), 1807–1822 (2012).
[CrossRef] [PubMed]

2011 (5)

S. A. Oladepo, K. Xiong, Z. Hong, and S. A. Asher, “Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy,” J. Phys. Chem. Lett.2(4), 334–344 (2011).
[CrossRef] [PubMed]

A. Kniggendorf, T. Gaul, and M. Meinhardt-Wollweber, “Hierarchical Cluster Analysis (HCA) of Microorganisms: An Assessment of Algorithms for Resonance Raman Spectra,” Appl. Spectrosc.65(2), 165–173 (2011).
[CrossRef]

S. Kecel, A. E. Ozel, S. Akyuz, S. Celik, and G. Agaeva, “Conformational analysis and vibrational spectroscopic investigation of L-proline-tyrosine (L-Pro-Tyr) dipeptide,” J. Mol. Struct.993(1-3), 349–356 (2011).
[CrossRef]

N. K. Budhavaram and J. R. Barone, “Quantifying amino acid and protein substitution using Raman spectroscopy,” J. Raman Spectrosc.42(3), 355–362 (2011).
[CrossRef]

A. G. Lee, “Lipid-protein interactions,” Biochem. Soc. Trans.39(3), 761–766 (2011).
[PubMed]

2010 (3)

H. A. Sánchez, G. Mese, M. Srinivas, T. W. White, and V. K. Verselis, “Differentially altered Ca2+ regulation and Ca2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome,” J. Gen. Physiol.136(1), 47–62 (2010).
[CrossRef] [PubMed]

H. S. Shafaat, B. S. Leigh, M. J. Tauber, and J. E. Kim, “Spectroscopic Comparison of Photogenerated Tryptophan Radicals in Azurin: Effects of Local Environment and Structure,” J. Am. Chem. Soc.132(26), 9030–9039 (2010).
[CrossRef] [PubMed]

C. Ambrosi, D. Boassa, J. Pranskevich, A. Smock, A. Oshima, J. Xu, B. J. Nicholson, and G. E. Sosinsky, “Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability,” Biophys. J.98(9), 1809–1819 (2010).
[CrossRef] [PubMed]

2009 (1)

S. Maeda, S. Nakagawa, M. Suga, E. Yamashita, A. Oshima, Y. Fujiyoshi, and T. Tsukihara, “Structure of the connexin 26 gap junction channel at 3.5 A resolution,” Nature458(7238), 597–602 (2009).
[CrossRef] [PubMed]

2008 (1)

M. Steffens, F. Göpel, A. Ngezahayo, C. Zeilinger, A. Ernst, and H. A. Kolb, “Regulation of connexons composed of human connexin26 (hCx26) by temperature,” Biochim. Biophys. Acta1778(5), 1206–1212 (2008).
[CrossRef] [PubMed]

2005 (3)

C. Zeilinger, M. Steffens, and H. A. Kolb, “Length of C-terminus of rCx46 influences oligomerization and hemichannel properties,” Biochim. Biophys. Acta1720(1-2), 35–43 (2005).
[CrossRef] [PubMed]

A. L. Jenkins, R. A. Larsen, and T. B. Williams, “Characterization of amino acids using Raman spectroscopy,” Spectrochim. Acta A Mol. Biomol. Spectrosc.61(7), 1585–1594 (2005).
[CrossRef] [PubMed]

C. Hunte, “Specific protein-lipid interactions in membrane proteins,” Biochem. Soc. Trans.33(5), 938–942 (2005).
[CrossRef] [PubMed]

2004 (4)

E. Podstawka, Y. Ozaki, and L. M. Proniewicz, “Part I: Surface-Enhanced Raman Spectroscopy Investigation of Amino Acids and Their Homodipeptides Adsorbed on Colloidal Silver,” Appl. Spectrosc.58(5), 570–580 (2004).
[CrossRef] [PubMed]

L. B. Faria, F. M. Almeida, O. Pilla, F. Rossi, J. M. Sasaki, F. E. A. Melo, J. Mendes Filho, and P. T. C. Freire, “Raman spectra of L-histidine hydrochloride monohydrate crystal,” J. Raman Spectrosc.35(3), 242–248 (2004).
[CrossRef]

C. Peracchia, “Chemical gating of gap junction channels; roles of calcium, pH and calmodulin,” Biochim. Biophys. Acta1662(1-2), 61–80 (2004).
[CrossRef] [PubMed]

F. F. Bukauskas and V. K. Verselis, “Gap junction channel gating,” Biochim. Biophys. Acta1662(1-2), 42–60 (2004).
[CrossRef] [PubMed]

2003 (1)

I. H. McColl, E. W. Blanch, A. C. Gill, A. G. Rhie, M. A. Ritchie, L. Hecht, K. Nielsen, and L. D. Barron, “A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(L-lysine) to the Prion Protein,” J. Am. Chem. Soc.125(33), 10019–10026 (2003).
[CrossRef] [PubMed]

2002 (2)

G. M. Hand, D. J. Müller, B. J. Nicholson, A. Engel, and G. E. Sosinsky, “Isolation and characterization of gap junctions from tissue culture cells,” J. Mol. Biol.315(4), 587–600 (2002).
[CrossRef] [PubMed]

D. L. Beahm and J. E. Hall, “Hemichannel and junctional properties of connexin 50,” Biophys. J.82(4), 2016–2031 (2002).
[CrossRef] [PubMed]

2001 (1)

A. Ianoul, M. N. Boyden, and S. A. Asher, “Dependence of the Peptide Amide III Vibration on the Φ Dihedral Angle,” J. Am. Chem. Soc.123(30), 7433–7434 (2001).
[CrossRef] [PubMed]

1992 (1)

J. Bandekar, “Amide modes and protein conformation,” Biochim. Biophys. Acta1120(2), 123–143 (1992).
[CrossRef] [PubMed]

1974 (1)

M. C. Chen and R. C. Lord, “Laser-Excited Raman Spectroscopy of Biomolecules. VI. Some Polypeptides as Conformational Models,” J. Am. Chem. Soc.96(15), 4750–4752 (1974).
[CrossRef] [PubMed]

1973 (1)

N.-T. Yu, B. H. Jo, and D. C. O’Shea, “Laser Raman Scattering of Cobramine B, a Basic Protein from Cobra Venom,” Arch. Biochem. Biophys.156(1), 71–76 (1973).
[CrossRef] [PubMed]

Agaeva, G.

S. Kecel, A. E. Ozel, S. Akyuz, S. Celik, and G. Agaeva, “Conformational analysis and vibrational spectroscopic investigation of L-proline-tyrosine (L-Pro-Tyr) dipeptide,” J. Mol. Struct.993(1-3), 349–356 (2011).
[CrossRef]

Akyuz, S.

S. Kecel, A. E. Ozel, S. Akyuz, S. Celik, and G. Agaeva, “Conformational analysis and vibrational spectroscopic investigation of L-proline-tyrosine (L-Pro-Tyr) dipeptide,” J. Mol. Struct.993(1-3), 349–356 (2011).
[CrossRef]

Almeida, F. M.

L. B. Faria, F. M. Almeida, O. Pilla, F. Rossi, J. M. Sasaki, F. E. A. Melo, J. Mendes Filho, and P. T. C. Freire, “Raman spectra of L-histidine hydrochloride monohydrate crystal,” J. Raman Spectrosc.35(3), 242–248 (2004).
[CrossRef]

Ambrosi, C.

C. Ambrosi, D. Boassa, J. Pranskevich, A. Smock, A. Oshima, J. Xu, B. J. Nicholson, and G. E. Sosinsky, “Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability,” Biophys. J.98(9), 1809–1819 (2010).
[CrossRef] [PubMed]

Asher, S. A.

S. A. Oladepo, K. Xiong, Z. Hong, and S. A. Asher, “Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy,” J. Phys. Chem. Lett.2(4), 334–344 (2011).
[CrossRef] [PubMed]

A. Ianoul, M. N. Boyden, and S. A. Asher, “Dependence of the Peptide Amide III Vibration on the Φ Dihedral Angle,” J. Am. Chem. Soc.123(30), 7433–7434 (2001).
[CrossRef] [PubMed]

Bandekar, J.

J. Bandekar, “Amide modes and protein conformation,” Biochim. Biophys. Acta1120(2), 123–143 (1992).
[CrossRef] [PubMed]

Baranska, M.

A. Rygula, K. Majzner, K. M. Marzec, A. Kaczor, M. Pilarczyk, and M. Baranska, “Raman spectroscopy of proteins: a review,” J. Raman Spectrosc.44(8), 1061–1076 (2013).
[CrossRef]

Bargiello, T. A.

T. A. Bargiello, Q. Tang, S. Oh, and T. Kwon, “Voltage-dependent conformational changes in connexin channels,” Biochim. Biophys. Acta1818(8), 1807–1822 (2012).
[CrossRef] [PubMed]

T. Kwon, B. Roux, S. Jo, J. B. Klauda, A. L. Harris, and T. A. Bargiello, “Molecular dynamics simulations of the Cx26 hemichannel: insights into voltage-dependent loop-gating,” Biophys. J.102(6), 1341–1351 (2012).
[CrossRef] [PubMed]

Barone, J. R.

N. K. Budhavaram and J. R. Barone, “Quantifying amino acid and protein substitution using Raman spectroscopy,” J. Raman Spectrosc.42(3), 355–362 (2011).
[CrossRef]

Barron, L. D.

I. H. McColl, E. W. Blanch, A. C. Gill, A. G. Rhie, M. A. Ritchie, L. Hecht, K. Nielsen, and L. D. Barron, “A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(L-lysine) to the Prion Protein,” J. Am. Chem. Soc.125(33), 10019–10026 (2003).
[CrossRef] [PubMed]

Beahm, D. L.

D. L. Beahm and J. E. Hall, “Hemichannel and junctional properties of connexin 50,” Biophys. J.82(4), 2016–2031 (2002).
[CrossRef] [PubMed]

Blanch, E. W.

I. H. McColl, E. W. Blanch, A. C. Gill, A. G. Rhie, M. A. Ritchie, L. Hecht, K. Nielsen, and L. D. Barron, “A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(L-lysine) to the Prion Protein,” J. Am. Chem. Soc.125(33), 10019–10026 (2003).
[CrossRef] [PubMed]

Boassa, D.

C. Ambrosi, D. Boassa, J. Pranskevich, A. Smock, A. Oshima, J. Xu, B. J. Nicholson, and G. E. Sosinsky, “Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability,” Biophys. J.98(9), 1809–1819 (2010).
[CrossRef] [PubMed]

Bortolozzi, M.

F. Zonta, G. Polles, M. F. Sanasi, M. Bortolozzi, and F. Mammano, “The 3.5 ångström X-ray structure of the human connexin26 gap junction channel is unlikely that of a fully open channel,” Cell Commun. Signal.11(1), 15 (2013), http://www.biosignaling.com/content/pdf/1478-811X-11-15.pdf .
[CrossRef] [PubMed]

Boyden, M. N.

A. Ianoul, M. N. Boyden, and S. A. Asher, “Dependence of the Peptide Amide III Vibration on the Φ Dihedral Angle,” J. Am. Chem. Soc.123(30), 7433–7434 (2001).
[CrossRef] [PubMed]

Budhavaram, N. K.

N. K. Budhavaram and J. R. Barone, “Quantifying amino acid and protein substitution using Raman spectroscopy,” J. Raman Spectrosc.42(3), 355–362 (2011).
[CrossRef]

Bukauskas, F. F.

F. F. Bukauskas and V. K. Verselis, “Gap junction channel gating,” Biochim. Biophys. Acta1662(1-2), 42–60 (2004).
[CrossRef] [PubMed]

Celik, S.

S. Kecel, A. E. Ozel, S. Akyuz, S. Celik, and G. Agaeva, “Conformational analysis and vibrational spectroscopic investigation of L-proline-tyrosine (L-Pro-Tyr) dipeptide,” J. Mol. Struct.993(1-3), 349–356 (2011).
[CrossRef]

Chen, M. C.

M. C. Chen and R. C. Lord, “Laser-Excited Raman Spectroscopy of Biomolecules. VI. Some Polypeptides as Conformational Models,” J. Am. Chem. Soc.96(15), 4750–4752 (1974).
[CrossRef] [PubMed]

Edwards, H. G. M.

J. Jehlička, A. Oren, and H. G. M. Edwards, “Raman spectra of osmotic solutes of halophiles,” J. Raman Spectrosc.43(8), 1134–1140 (2012).
[CrossRef]

Engel, A.

G. M. Hand, D. J. Müller, B. J. Nicholson, A. Engel, and G. E. Sosinsky, “Isolation and characterization of gap junctions from tissue culture cells,” J. Mol. Biol.315(4), 587–600 (2002).
[CrossRef] [PubMed]

Ernst, A.

M. Steffens, F. Göpel, A. Ngezahayo, C. Zeilinger, A. Ernst, and H. A. Kolb, “Regulation of connexons composed of human connexin26 (hCx26) by temperature,” Biochim. Biophys. Acta1778(5), 1206–1212 (2008).
[CrossRef] [PubMed]

Faria, L. B.

L. B. Faria, F. M. Almeida, O. Pilla, F. Rossi, J. M. Sasaki, F. E. A. Melo, J. Mendes Filho, and P. T. C. Freire, “Raman spectra of L-histidine hydrochloride monohydrate crystal,” J. Raman Spectrosc.35(3), 242–248 (2004).
[CrossRef]

Freire, P. T. C.

G. P. Sousa, P. T. C. Freire, J. Mendes Filho, F. E. A. Melo, and C. L. Lima, “Low-Temperature Raman Spectra of L-Histidine Crystals,” Braz. J. Phys.43(3), 137–144 (2013).
[CrossRef]

L. B. Faria, F. M. Almeida, O. Pilla, F. Rossi, J. M. Sasaki, F. E. A. Melo, J. Mendes Filho, and P. T. C. Freire, “Raman spectra of L-histidine hydrochloride monohydrate crystal,” J. Raman Spectrosc.35(3), 242–248 (2004).
[CrossRef]

Fujiyoshi, Y.

S. Maeda, S. Nakagawa, M. Suga, E. Yamashita, A. Oshima, Y. Fujiyoshi, and T. Tsukihara, “Structure of the connexin 26 gap junction channel at 3.5 A resolution,” Nature458(7238), 597–602 (2009).
[CrossRef] [PubMed]

Gaul, T.

Gill, A. C.

I. H. McColl, E. W. Blanch, A. C. Gill, A. G. Rhie, M. A. Ritchie, L. Hecht, K. Nielsen, and L. D. Barron, “A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(L-lysine) to the Prion Protein,” J. Am. Chem. Soc.125(33), 10019–10026 (2003).
[CrossRef] [PubMed]

Göpel, F.

M. Steffens, F. Göpel, A. Ngezahayo, C. Zeilinger, A. Ernst, and H. A. Kolb, “Regulation of connexons composed of human connexin26 (hCx26) by temperature,” Biochim. Biophys. Acta1778(5), 1206–1212 (2008).
[CrossRef] [PubMed]

Hall, J. E.

D. L. Beahm and J. E. Hall, “Hemichannel and junctional properties of connexin 50,” Biophys. J.82(4), 2016–2031 (2002).
[CrossRef] [PubMed]

Hand, G. M.

G. M. Hand, D. J. Müller, B. J. Nicholson, A. Engel, and G. E. Sosinsky, “Isolation and characterization of gap junctions from tissue culture cells,” J. Mol. Biol.315(4), 587–600 (2002).
[CrossRef] [PubMed]

Harris, A. L.

T. Kwon, B. Roux, S. Jo, J. B. Klauda, A. L. Harris, and T. A. Bargiello, “Molecular dynamics simulations of the Cx26 hemichannel: insights into voltage-dependent loop-gating,” Biophys. J.102(6), 1341–1351 (2012).
[CrossRef] [PubMed]

Hecht, L.

I. H. McColl, E. W. Blanch, A. C. Gill, A. G. Rhie, M. A. Ritchie, L. Hecht, K. Nielsen, and L. D. Barron, “A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(L-lysine) to the Prion Protein,” J. Am. Chem. Soc.125(33), 10019–10026 (2003).
[CrossRef] [PubMed]

Hong, Z.

S. A. Oladepo, K. Xiong, Z. Hong, and S. A. Asher, “Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy,” J. Phys. Chem. Lett.2(4), 334–344 (2011).
[CrossRef] [PubMed]

Hunte, C.

C. Hunte, “Specific protein-lipid interactions in membrane proteins,” Biochem. Soc. Trans.33(5), 938–942 (2005).
[CrossRef] [PubMed]

Ianoul, A.

A. Ianoul, M. N. Boyden, and S. A. Asher, “Dependence of the Peptide Amide III Vibration on the Φ Dihedral Angle,” J. Am. Chem. Soc.123(30), 7433–7434 (2001).
[CrossRef] [PubMed]

Jehlicka, J.

J. Jehlička, A. Oren, and H. G. M. Edwards, “Raman spectra of osmotic solutes of halophiles,” J. Raman Spectrosc.43(8), 1134–1140 (2012).
[CrossRef]

Jenkins, A. L.

A. L. Jenkins, R. A. Larsen, and T. B. Williams, “Characterization of amino acids using Raman spectroscopy,” Spectrochim. Acta A Mol. Biomol. Spectrosc.61(7), 1585–1594 (2005).
[CrossRef] [PubMed]

Jo, B. H.

N.-T. Yu, B. H. Jo, and D. C. O’Shea, “Laser Raman Scattering of Cobramine B, a Basic Protein from Cobra Venom,” Arch. Biochem. Biophys.156(1), 71–76 (1973).
[CrossRef] [PubMed]

Jo, S.

T. Kwon, B. Roux, S. Jo, J. B. Klauda, A. L. Harris, and T. A. Bargiello, “Molecular dynamics simulations of the Cx26 hemichannel: insights into voltage-dependent loop-gating,” Biophys. J.102(6), 1341–1351 (2012).
[CrossRef] [PubMed]

Kaczor, A.

A. Rygula, K. Majzner, K. M. Marzec, A. Kaczor, M. Pilarczyk, and M. Baranska, “Raman spectroscopy of proteins: a review,” J. Raman Spectrosc.44(8), 1061–1076 (2013).
[CrossRef]

Kecel, S.

S. Kecel, A. E. Ozel, S. Akyuz, S. Celik, and G. Agaeva, “Conformational analysis and vibrational spectroscopic investigation of L-proline-tyrosine (L-Pro-Tyr) dipeptide,” J. Mol. Struct.993(1-3), 349–356 (2011).
[CrossRef]

Kim, J. E.

H. S. Shafaat, B. S. Leigh, M. J. Tauber, and J. E. Kim, “Spectroscopic Comparison of Photogenerated Tryptophan Radicals in Azurin: Effects of Local Environment and Structure,” J. Am. Chem. Soc.132(26), 9030–9039 (2010).
[CrossRef] [PubMed]

Klauda, J. B.

T. Kwon, B. Roux, S. Jo, J. B. Klauda, A. L. Harris, and T. A. Bargiello, “Molecular dynamics simulations of the Cx26 hemichannel: insights into voltage-dependent loop-gating,” Biophys. J.102(6), 1341–1351 (2012).
[CrossRef] [PubMed]

Kniggendorf, A.

Kolb, H. A.

M. Steffens, F. Göpel, A. Ngezahayo, C. Zeilinger, A. Ernst, and H. A. Kolb, “Regulation of connexons composed of human connexin26 (hCx26) by temperature,” Biochim. Biophys. Acta1778(5), 1206–1212 (2008).
[CrossRef] [PubMed]

C. Zeilinger, M. Steffens, and H. A. Kolb, “Length of C-terminus of rCx46 influences oligomerization and hemichannel properties,” Biochim. Biophys. Acta1720(1-2), 35–43 (2005).
[CrossRef] [PubMed]

Kwon, T.

T. A. Bargiello, Q. Tang, S. Oh, and T. Kwon, “Voltage-dependent conformational changes in connexin channels,” Biochim. Biophys. Acta1818(8), 1807–1822 (2012).
[CrossRef] [PubMed]

T. Kwon, B. Roux, S. Jo, J. B. Klauda, A. L. Harris, and T. A. Bargiello, “Molecular dynamics simulations of the Cx26 hemichannel: insights into voltage-dependent loop-gating,” Biophys. J.102(6), 1341–1351 (2012).
[CrossRef] [PubMed]

Larsen, R. A.

A. L. Jenkins, R. A. Larsen, and T. B. Williams, “Characterization of amino acids using Raman spectroscopy,” Spectrochim. Acta A Mol. Biomol. Spectrosc.61(7), 1585–1594 (2005).
[CrossRef] [PubMed]

Lee, A. G.

A. G. Lee, “Lipid-protein interactions,” Biochem. Soc. Trans.39(3), 761–766 (2011).
[PubMed]

Leigh, B. S.

H. S. Shafaat, B. S. Leigh, M. J. Tauber, and J. E. Kim, “Spectroscopic Comparison of Photogenerated Tryptophan Radicals in Azurin: Effects of Local Environment and Structure,” J. Am. Chem. Soc.132(26), 9030–9039 (2010).
[CrossRef] [PubMed]

Lima, C. L.

G. P. Sousa, P. T. C. Freire, J. Mendes Filho, F. E. A. Melo, and C. L. Lima, “Low-Temperature Raman Spectra of L-Histidine Crystals,” Braz. J. Phys.43(3), 137–144 (2013).
[CrossRef]

Lord, R. C.

M. C. Chen and R. C. Lord, “Laser-Excited Raman Spectroscopy of Biomolecules. VI. Some Polypeptides as Conformational Models,” J. Am. Chem. Soc.96(15), 4750–4752 (1974).
[CrossRef] [PubMed]

Maeda, S.

S. Maeda, S. Nakagawa, M. Suga, E. Yamashita, A. Oshima, Y. Fujiyoshi, and T. Tsukihara, “Structure of the connexin 26 gap junction channel at 3.5 A resolution,” Nature458(7238), 597–602 (2009).
[CrossRef] [PubMed]

Majzner, K.

A. Rygula, K. Majzner, K. M. Marzec, A. Kaczor, M. Pilarczyk, and M. Baranska, “Raman spectroscopy of proteins: a review,” J. Raman Spectrosc.44(8), 1061–1076 (2013).
[CrossRef]

Mammano, F.

F. Zonta, G. Polles, M. F. Sanasi, M. Bortolozzi, and F. Mammano, “The 3.5 ångström X-ray structure of the human connexin26 gap junction channel is unlikely that of a fully open channel,” Cell Commun. Signal.11(1), 15 (2013), http://www.biosignaling.com/content/pdf/1478-811X-11-15.pdf .
[CrossRef] [PubMed]

F. Zonta, G. Polles, G. Zanotti, and F. Mammano, “Permeation pathway of homomeric connexin 26 and connexin 30 channels investigated by molecular dynamics,” J. Biomol. Struct. Dyn.29(5), 985–998 (2012).
[CrossRef] [PubMed]

Marzec, K. M.

A. Rygula, K. Majzner, K. M. Marzec, A. Kaczor, M. Pilarczyk, and M. Baranska, “Raman spectroscopy of proteins: a review,” J. Raman Spectrosc.44(8), 1061–1076 (2013).
[CrossRef]

McColl, I. H.

I. H. McColl, E. W. Blanch, A. C. Gill, A. G. Rhie, M. A. Ritchie, L. Hecht, K. Nielsen, and L. D. Barron, “A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(L-lysine) to the Prion Protein,” J. Am. Chem. Soc.125(33), 10019–10026 (2003).
[CrossRef] [PubMed]

Meinhardt-Wollweber, M.

Melo, F. E. A.

G. P. Sousa, P. T. C. Freire, J. Mendes Filho, F. E. A. Melo, and C. L. Lima, “Low-Temperature Raman Spectra of L-Histidine Crystals,” Braz. J. Phys.43(3), 137–144 (2013).
[CrossRef]

L. B. Faria, F. M. Almeida, O. Pilla, F. Rossi, J. M. Sasaki, F. E. A. Melo, J. Mendes Filho, and P. T. C. Freire, “Raman spectra of L-histidine hydrochloride monohydrate crystal,” J. Raman Spectrosc.35(3), 242–248 (2004).
[CrossRef]

Mendes Filho, J.

G. P. Sousa, P. T. C. Freire, J. Mendes Filho, F. E. A. Melo, and C. L. Lima, “Low-Temperature Raman Spectra of L-Histidine Crystals,” Braz. J. Phys.43(3), 137–144 (2013).
[CrossRef]

L. B. Faria, F. M. Almeida, O. Pilla, F. Rossi, J. M. Sasaki, F. E. A. Melo, J. Mendes Filho, and P. T. C. Freire, “Raman spectra of L-histidine hydrochloride monohydrate crystal,” J. Raman Spectrosc.35(3), 242–248 (2004).
[CrossRef]

Mese, G.

H. A. Sánchez, G. Mese, M. Srinivas, T. W. White, and V. K. Verselis, “Differentially altered Ca2+ regulation and Ca2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome,” J. Gen. Physiol.136(1), 47–62 (2010).
[CrossRef] [PubMed]

Müller, D. J.

G. M. Hand, D. J. Müller, B. J. Nicholson, A. Engel, and G. E. Sosinsky, “Isolation and characterization of gap junctions from tissue culture cells,” J. Mol. Biol.315(4), 587–600 (2002).
[CrossRef] [PubMed]

Nakagawa, S.

S. Maeda, S. Nakagawa, M. Suga, E. Yamashita, A. Oshima, Y. Fujiyoshi, and T. Tsukihara, “Structure of the connexin 26 gap junction channel at 3.5 A resolution,” Nature458(7238), 597–602 (2009).
[CrossRef] [PubMed]

Ngezahayo, A.

M. Steffens, F. Göpel, A. Ngezahayo, C. Zeilinger, A. Ernst, and H. A. Kolb, “Regulation of connexons composed of human connexin26 (hCx26) by temperature,” Biochim. Biophys. Acta1778(5), 1206–1212 (2008).
[CrossRef] [PubMed]

Nicholson, B. J.

C. Ambrosi, D. Boassa, J. Pranskevich, A. Smock, A. Oshima, J. Xu, B. J. Nicholson, and G. E. Sosinsky, “Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability,” Biophys. J.98(9), 1809–1819 (2010).
[CrossRef] [PubMed]

G. M. Hand, D. J. Müller, B. J. Nicholson, A. Engel, and G. E. Sosinsky, “Isolation and characterization of gap junctions from tissue culture cells,” J. Mol. Biol.315(4), 587–600 (2002).
[CrossRef] [PubMed]

Nielsen, K.

I. H. McColl, E. W. Blanch, A. C. Gill, A. G. Rhie, M. A. Ritchie, L. Hecht, K. Nielsen, and L. D. Barron, “A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(L-lysine) to the Prion Protein,” J. Am. Chem. Soc.125(33), 10019–10026 (2003).
[CrossRef] [PubMed]

O’Shea, D. C.

N.-T. Yu, B. H. Jo, and D. C. O’Shea, “Laser Raman Scattering of Cobramine B, a Basic Protein from Cobra Venom,” Arch. Biochem. Biophys.156(1), 71–76 (1973).
[CrossRef] [PubMed]

Oh, S.

T. A. Bargiello, Q. Tang, S. Oh, and T. Kwon, “Voltage-dependent conformational changes in connexin channels,” Biochim. Biophys. Acta1818(8), 1807–1822 (2012).
[CrossRef] [PubMed]

Oladepo, S. A.

S. A. Oladepo, K. Xiong, Z. Hong, and S. A. Asher, “Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy,” J. Phys. Chem. Lett.2(4), 334–344 (2011).
[CrossRef] [PubMed]

Oren, A.

J. Jehlička, A. Oren, and H. G. M. Edwards, “Raman spectra of osmotic solutes of halophiles,” J. Raman Spectrosc.43(8), 1134–1140 (2012).
[CrossRef]

Oshima, A.

C. Ambrosi, D. Boassa, J. Pranskevich, A. Smock, A. Oshima, J. Xu, B. J. Nicholson, and G. E. Sosinsky, “Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability,” Biophys. J.98(9), 1809–1819 (2010).
[CrossRef] [PubMed]

S. Maeda, S. Nakagawa, M. Suga, E. Yamashita, A. Oshima, Y. Fujiyoshi, and T. Tsukihara, “Structure of the connexin 26 gap junction channel at 3.5 A resolution,” Nature458(7238), 597–602 (2009).
[CrossRef] [PubMed]

Ozaki, Y.

Ozel, A. E.

S. Kecel, A. E. Ozel, S. Akyuz, S. Celik, and G. Agaeva, “Conformational analysis and vibrational spectroscopic investigation of L-proline-tyrosine (L-Pro-Tyr) dipeptide,” J. Mol. Struct.993(1-3), 349–356 (2011).
[CrossRef]

Peracchia, C.

C. Peracchia, “Chemical gating of gap junction channels; roles of calcium, pH and calmodulin,” Biochim. Biophys. Acta1662(1-2), 61–80 (2004).
[CrossRef] [PubMed]

Pilarczyk, M.

A. Rygula, K. Majzner, K. M. Marzec, A. Kaczor, M. Pilarczyk, and M. Baranska, “Raman spectroscopy of proteins: a review,” J. Raman Spectrosc.44(8), 1061–1076 (2013).
[CrossRef]

Pilla, O.

L. B. Faria, F. M. Almeida, O. Pilla, F. Rossi, J. M. Sasaki, F. E. A. Melo, J. Mendes Filho, and P. T. C. Freire, “Raman spectra of L-histidine hydrochloride monohydrate crystal,” J. Raman Spectrosc.35(3), 242–248 (2004).
[CrossRef]

Podstawka, E.

Polles, G.

F. Zonta, G. Polles, M. F. Sanasi, M. Bortolozzi, and F. Mammano, “The 3.5 ångström X-ray structure of the human connexin26 gap junction channel is unlikely that of a fully open channel,” Cell Commun. Signal.11(1), 15 (2013), http://www.biosignaling.com/content/pdf/1478-811X-11-15.pdf .
[CrossRef] [PubMed]

F. Zonta, G. Polles, G. Zanotti, and F. Mammano, “Permeation pathway of homomeric connexin 26 and connexin 30 channels investigated by molecular dynamics,” J. Biomol. Struct. Dyn.29(5), 985–998 (2012).
[CrossRef] [PubMed]

Pranskevich, J.

C. Ambrosi, D. Boassa, J. Pranskevich, A. Smock, A. Oshima, J. Xu, B. J. Nicholson, and G. E. Sosinsky, “Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability,” Biophys. J.98(9), 1809–1819 (2010).
[CrossRef] [PubMed]

Proniewicz, L. M.

Rhie, A. G.

I. H. McColl, E. W. Blanch, A. C. Gill, A. G. Rhie, M. A. Ritchie, L. Hecht, K. Nielsen, and L. D. Barron, “A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(L-lysine) to the Prion Protein,” J. Am. Chem. Soc.125(33), 10019–10026 (2003).
[CrossRef] [PubMed]

Ritchie, M. A.

I. H. McColl, E. W. Blanch, A. C. Gill, A. G. Rhie, M. A. Ritchie, L. Hecht, K. Nielsen, and L. D. Barron, “A New Perspective on β-Sheet Structures Using Vibrational Raman Optical Activity: From Poly(L-lysine) to the Prion Protein,” J. Am. Chem. Soc.125(33), 10019–10026 (2003).
[CrossRef] [PubMed]

Rossi, F.

L. B. Faria, F. M. Almeida, O. Pilla, F. Rossi, J. M. Sasaki, F. E. A. Melo, J. Mendes Filho, and P. T. C. Freire, “Raman spectra of L-histidine hydrochloride monohydrate crystal,” J. Raman Spectrosc.35(3), 242–248 (2004).
[CrossRef]

Roux, B.

T. Kwon, B. Roux, S. Jo, J. B. Klauda, A. L. Harris, and T. A. Bargiello, “Molecular dynamics simulations of the Cx26 hemichannel: insights into voltage-dependent loop-gating,” Biophys. J.102(6), 1341–1351 (2012).
[CrossRef] [PubMed]

Rygula, A.

A. Rygula, K. Majzner, K. M. Marzec, A. Kaczor, M. Pilarczyk, and M. Baranska, “Raman spectroscopy of proteins: a review,” J. Raman Spectrosc.44(8), 1061–1076 (2013).
[CrossRef]

Sanasi, M. F.

F. Zonta, G. Polles, M. F. Sanasi, M. Bortolozzi, and F. Mammano, “The 3.5 ångström X-ray structure of the human connexin26 gap junction channel is unlikely that of a fully open channel,” Cell Commun. Signal.11(1), 15 (2013), http://www.biosignaling.com/content/pdf/1478-811X-11-15.pdf .
[CrossRef] [PubMed]

Sánchez, H. A.

H. A. Sánchez, G. Mese, M. Srinivas, T. W. White, and V. K. Verselis, “Differentially altered Ca2+ regulation and Ca2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome,” J. Gen. Physiol.136(1), 47–62 (2010).
[CrossRef] [PubMed]

Sasaki, J. M.

L. B. Faria, F. M. Almeida, O. Pilla, F. Rossi, J. M. Sasaki, F. E. A. Melo, J. Mendes Filho, and P. T. C. Freire, “Raman spectra of L-histidine hydrochloride monohydrate crystal,” J. Raman Spectrosc.35(3), 242–248 (2004).
[CrossRef]

Shafaat, H. S.

H. S. Shafaat, B. S. Leigh, M. J. Tauber, and J. E. Kim, “Spectroscopic Comparison of Photogenerated Tryptophan Radicals in Azurin: Effects of Local Environment and Structure,” J. Am. Chem. Soc.132(26), 9030–9039 (2010).
[CrossRef] [PubMed]

Smock, A.

C. Ambrosi, D. Boassa, J. Pranskevich, A. Smock, A. Oshima, J. Xu, B. J. Nicholson, and G. E. Sosinsky, “Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability,” Biophys. J.98(9), 1809–1819 (2010).
[CrossRef] [PubMed]

Sosinsky, G. E.

C. Ambrosi, D. Boassa, J. Pranskevich, A. Smock, A. Oshima, J. Xu, B. J. Nicholson, and G. E. Sosinsky, “Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability,” Biophys. J.98(9), 1809–1819 (2010).
[CrossRef] [PubMed]

G. M. Hand, D. J. Müller, B. J. Nicholson, A. Engel, and G. E. Sosinsky, “Isolation and characterization of gap junctions from tissue culture cells,” J. Mol. Biol.315(4), 587–600 (2002).
[CrossRef] [PubMed]

Sousa, G. P.

G. P. Sousa, P. T. C. Freire, J. Mendes Filho, F. E. A. Melo, and C. L. Lima, “Low-Temperature Raman Spectra of L-Histidine Crystals,” Braz. J. Phys.43(3), 137–144 (2013).
[CrossRef]

Srinivas, M.

H. A. Sánchez, G. Mese, M. Srinivas, T. W. White, and V. K. Verselis, “Differentially altered Ca2+ regulation and Ca2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome,” J. Gen. Physiol.136(1), 47–62 (2010).
[CrossRef] [PubMed]

Steffens, M.

M. Steffens, F. Göpel, A. Ngezahayo, C. Zeilinger, A. Ernst, and H. A. Kolb, “Regulation of connexons composed of human connexin26 (hCx26) by temperature,” Biochim. Biophys. Acta1778(5), 1206–1212 (2008).
[CrossRef] [PubMed]

C. Zeilinger, M. Steffens, and H. A. Kolb, “Length of C-terminus of rCx46 influences oligomerization and hemichannel properties,” Biochim. Biophys. Acta1720(1-2), 35–43 (2005).
[CrossRef] [PubMed]

Suga, M.

S. Maeda, S. Nakagawa, M. Suga, E. Yamashita, A. Oshima, Y. Fujiyoshi, and T. Tsukihara, “Structure of the connexin 26 gap junction channel at 3.5 A resolution,” Nature458(7238), 597–602 (2009).
[CrossRef] [PubMed]

Tang, Q.

T. A. Bargiello, Q. Tang, S. Oh, and T. Kwon, “Voltage-dependent conformational changes in connexin channels,” Biochim. Biophys. Acta1818(8), 1807–1822 (2012).
[CrossRef] [PubMed]

Tauber, M. J.

H. S. Shafaat, B. S. Leigh, M. J. Tauber, and J. E. Kim, “Spectroscopic Comparison of Photogenerated Tryptophan Radicals in Azurin: Effects of Local Environment and Structure,” J. Am. Chem. Soc.132(26), 9030–9039 (2010).
[CrossRef] [PubMed]

Tsukihara, T.

S. Maeda, S. Nakagawa, M. Suga, E. Yamashita, A. Oshima, Y. Fujiyoshi, and T. Tsukihara, “Structure of the connexin 26 gap junction channel at 3.5 A resolution,” Nature458(7238), 597–602 (2009).
[CrossRef] [PubMed]

Verselis, V. K.

H. A. Sánchez, G. Mese, M. Srinivas, T. W. White, and V. K. Verselis, “Differentially altered Ca2+ regulation and Ca2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome,” J. Gen. Physiol.136(1), 47–62 (2010).
[CrossRef] [PubMed]

F. F. Bukauskas and V. K. Verselis, “Gap junction channel gating,” Biochim. Biophys. Acta1662(1-2), 42–60 (2004).
[CrossRef] [PubMed]

White, T. W.

H. A. Sánchez, G. Mese, M. Srinivas, T. W. White, and V. K. Verselis, “Differentially altered Ca2+ regulation and Ca2+ permeability in Cx26 hemichannels formed by the A40V and G45E mutations that cause keratitis ichthyosis deafness syndrome,” J. Gen. Physiol.136(1), 47–62 (2010).
[CrossRef] [PubMed]

Williams, T. B.

A. L. Jenkins, R. A. Larsen, and T. B. Williams, “Characterization of amino acids using Raman spectroscopy,” Spectrochim. Acta A Mol. Biomol. Spectrosc.61(7), 1585–1594 (2005).
[CrossRef] [PubMed]

Xiong, K.

S. A. Oladepo, K. Xiong, Z. Hong, and S. A. Asher, “Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy,” J. Phys. Chem. Lett.2(4), 334–344 (2011).
[CrossRef] [PubMed]

Xu, J.

C. Ambrosi, D. Boassa, J. Pranskevich, A. Smock, A. Oshima, J. Xu, B. J. Nicholson, and G. E. Sosinsky, “Analysis of four connexin26 mutant gap junctions and hemichannels reveals variations in hexamer stability,” Biophys. J.98(9), 1809–1819 (2010).
[CrossRef] [PubMed]

Yamashita, E.

S. Maeda, S. Nakagawa, M. Suga, E. Yamashita, A. Oshima, Y. Fujiyoshi, and T. Tsukihara, “Structure of the connexin 26 gap junction channel at 3.5 A resolution,” Nature458(7238), 597–602 (2009).
[CrossRef] [PubMed]

Yu, N.-T.

N.-T. Yu, B. H. Jo, and D. C. O’Shea, “Laser Raman Scattering of Cobramine B, a Basic Protein from Cobra Venom,” Arch. Biochem. Biophys.156(1), 71–76 (1973).
[CrossRef] [PubMed]

Zanotti, G.

F. Zonta, G. Polles, G. Zanotti, and F. Mammano, “Permeation pathway of homomeric connexin 26 and connexin 30 channels investigated by molecular dynamics,” J. Biomol. Struct. Dyn.29(5), 985–998 (2012).
[CrossRef] [PubMed]

Zeilinger, C.

M. Steffens, F. Göpel, A. Ngezahayo, C. Zeilinger, A. Ernst, and H. A. Kolb, “Regulation of connexons composed of human connexin26 (hCx26) by temperature,” Biochim. Biophys. Acta1778(5), 1206–1212 (2008).
[CrossRef] [PubMed]

C. Zeilinger, M. Steffens, and H. A. Kolb, “Length of C-terminus of rCx46 influences oligomerization and hemichannel properties,” Biochim. Biophys. Acta1720(1-2), 35–43 (2005).
[CrossRef] [PubMed]

Zonta, F.

F. Zonta, G. Polles, M. F. Sanasi, M. Bortolozzi, and F. Mammano, “The 3.5 ångström X-ray structure of the human connexin26 gap junction channel is unlikely that of a fully open channel,” Cell Commun. Signal.11(1), 15 (2013), http://www.biosignaling.com/content/pdf/1478-811X-11-15.pdf .
[CrossRef] [PubMed]

F. Zonta, G. Polles, G. Zanotti, and F. Mammano, “Permeation pathway of homomeric connexin 26 and connexin 30 channels investigated by molecular dynamics,” J. Biomol. Struct. Dyn.29(5), 985–998 (2012).
[CrossRef] [PubMed]

Appl. Spectrosc. (2)

Arch. Biochem. Biophys. (1)

N.-T. Yu, B. H. Jo, and D. C. O’Shea, “Laser Raman Scattering of Cobramine B, a Basic Protein from Cobra Venom,” Arch. Biochem. Biophys.156(1), 71–76 (1973).
[CrossRef] [PubMed]

Biochem. Soc. Trans. (2)

C. Hunte, “Specific protein-lipid interactions in membrane proteins,” Biochem. Soc. Trans.33(5), 938–942 (2005).
[CrossRef] [PubMed]

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Figures (6)

Fig. 1
Fig. 1

Cartoon of the hCx26 channel showing six protomers. A single protomer is emphasized in color with the plug in dark grey, TM1 (cyan), TM2-3 (grey), TM4 (blue), EL1 (yellow), EL2 (orange), and the parahelix in green. (Structural data: pdb database (PDB ID: 2ZW3); edited with PyMol 1.6.0.0; PyMol Executable Build Copyright by Schrodinger, LCC).

Fig. 2
Fig. 2

Single channel recording (SCR) after functional reconstitution of hCx26 into a planar bilayer. Single channel traces at different applied voltages at 19°C and 28°C after leak subtraction and corresponding point-amplitude histograms.

Fig. 3
Fig. 3

Raman spectrum of purified hCx26 protein in Ca2+-buffered POPC, recorded at 10°C (black) and 30°C (red). The average number of CCD counts per individual spectrum prior full-spectrum vector-normalization was 25000 counts (see Fig. 4 for the untreated spectra).

Fig. 4
Fig. 4

Raman spectra as recorded of purified hCx26 in detergent buffer at 10°C (green) and 30°C (yellow), of hCx26 in POPC at 10°C (blue) and 30°C (purple), and hCx26 in Ca2+-buffered POPC at 30°C (red). Note that these spectra differ solely by their total intensity. For an example of their spectral differences, see Fig. 5 (black spectrum).

Fig. 5
Fig. 5

Difference spectrum of purified hCx26 in POPC (black) and in Ca2+-buffered POPC at 10°C and 30°C (blue). The difference spectra prior smoothing are given in grey and cyan, respectively. Raman spectra recorded at 10°C were subtracted from the respective spectra recorded at 30°C.

Fig. 6
Fig. 6

Cartoon of the hCx26 protomer with the amino acids identified in the Raman spectrum given in colored stick representation: cysteine (magenta), histidine (yellow), lysine (blue), proline (cyan), and tyrosine (orange). EL1, EL2, parahelix, and plug are darkened for easier orientation with respect to Fig. 1. (Structural data obtained from the pdb database (PDB ID: 2ZW3); edited by Open-Source PyMOL 1.6.0.0; PyMOL Executable Build Copyright by Schrodinger, LLC.)

Tables (1)

Tables Icon

Table 1 Tentative assignment of Raman lines in the spectrum of hCx26

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