Folding and assembly of proteorhodopsin

被引：79

作者：

Klyszejko, Adriana L. ^{[1
]}

Shastri, Sarika ^{[2
,3
]}

Mari, Stefania A. ^{[4
]}

Grubmueller, Helmut ^{[5
]}

Muller, Daniel J. ^{[1
]}

Glaubitz, Clemens ^{[2
,3
]}

机构：

[1] Tech Univ Dresden, Ctr Biotechnol, D-8027 Dresden, Germany

[2] Goethe Univ Frankfurt, Inst Biophys Chem, Frankfurt, Germany

[3] Goethe Univ Frankfurt, Ctr Biomol Magnet Resonance, Frankfurt, Germany

[4] Univ Milan, Inst Gen Physiol & Biol Chem, I-20122 Milan, Italy

[5] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2008年 / 376卷 / 01期

关键词：

membrane protein folding; oligomeric state; hexamer; high-resolution atomic force microscopy; single-molecule force spectroscopy;

D O I：

10.1016/j.jmb.2007.11.030

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Proteorhodopsins (PRs), the recently discovered light-driven proton pumps, play a major role in supplying energy for microbial organisms of oceans. In contrast to PR, rhodopsins found in Archaea and Eukarya are structurally well characterized. Using single-molecule microscopy and spectroscopy, we observed the oligomeric assembly of native PR molecules and detected their folding in the membrane. PR showed unfolding patterns identical with those of bacteriorhodopsin and halorhodopsin, indicating that PR folds similarly to archaeal rhodopsins. Surprisingly, PR predominantly assembles into hexameric oligomers, with a smaller fraction assembling into pentamers. Within these oligomers, PR arranged into radial assemblies. We suggest that this structural assembly of PR may have functional implications. (C) 2007 Elsevier Ltd. All rights reserved.

引用

页码：35 / 41

页数：7

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