Immobility of phycobilins in the thylakoid lumen of a cryptophyte suggests that protein diffusion in the lumen is very restricted

被引：34

作者：

Kana, Radek ^{[1
,2
,3
]}

Prasil, Ondrej ^{[1
,2
,3
]}

Mullineaux, Conrad W. ^{[4
]}

机构：

[1] Acad Sci Czech Republ, Inst Microbiol, Trebon 37981, Czech Republic

[2] Univ S Bohemia Ceske Budejovice, Inst Phys Biol, Ceske Budejovice, Czech Republic

[3] Univ S Bohemia Ceske Budejovice, Fac Biol, Ceske Budejovice, Czech Republic

[4] Univ London, Sch Biol & Chem Sci, London E1 4NS, England

来源：

FEBS LETTERS | 2009年 / 583卷 / 04期

基金：

英国生物技术与生命科学研究理事会; 英国惠康基金;

关键词：

Cryptophyte (Rhodomonas salina); Fluorescence recovery after photobleaching; Protein diffusion; Thylakoid lumen; Phycobilin; Phycoerythrin; GREEN FLUORESCENT PROTEIN; PHOTOSYSTEM-II; LIGHT; MEMBRANES; CHLOROPLASTS; PLASTOCYANIN; ORGANIZATION; COMPLEXES; TRANSPORT; MOBILITY;

D O I：

10.1016/j.febslet.2009.01.016

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：

The thylakoid lumen is an important photosynthetic compartment which is the site of key steps in photosynthetic electron transport. The fluidity of the lumen could be a major constraint on photosynthetic electron transport rates. We used Fluorescence Recovery After Photobleaching in cells of the cryptophyte alga Rhodomonas salina to probe the diffusion of phycoerythrin in the lumen and chlorophyll complexes in the thylakoid membrane. In neither case was there any detectable diffusion over a timescale of several minutes. This indicates very restricted phycoerythrin mobility. This may be a general feature of protein diffusion in the thylakoid lumen. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：670 / 674

页数：5

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