Light-dependent cold-induced fatty acid unsaturation, changes in membrane fluidity, and alterations in gene expression in Synechocystis

被引:66
|
作者
Mironov, Kirill S. [1 ]
Sidorov, Roman A. [1 ]
Trofimova, Marina S. [1 ]
Bedbenov, Vladimir S. [1 ]
Tsydendambaev, Vladimir D. [1 ]
Allakhverdiev, Suleyman I. [1 ]
Los, Dmitry A. [1 ]
机构
[1] Russian Acad Sci, Inst Plant Physiol, Moscow 127276, Russia
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2012年 / 1817卷 / 08期
基金
俄罗斯基础研究基金会;
关键词
Synechocystis; Cold stress; Gene expression; Fatty acid desaturase; Membrane fluidity; Unsaturated fatty acid; CYANOBACTERIUM; TEMPERATURE; LIPIDS; PERCEPTION; SIGNAL; TRANSDUCTION; DESATURASES; ANISOTROPY; PCC-6803; SENSORS;
D O I
10.1016/j.bbabio.2011.12.011
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
Cold stress causes unsaturation of the membrane lipids. This leads to adjustment of the membrane fluidity, which is necessary for cold acclimation of cells. Here we demonstrate that the cold-induced accumulation of PUFAs in the cyanobacterium Synechocystis is light-dependent. The desA(-)/desD(-) mutant, that lacks the genes for Delta 2 and Delta 6 desaturases, is still able to adjust the fluidity of its membranes in spite of its inability to synthesize PUFAs and modulate the fatty acid composition of the membrane lipids under cold stress. The expression of cold-induced genes, which are controlled by the cold sensor histidine kinase Hik33, depends on the fluidity of cell membranes and it is regulated by light, though it does not require the activity of the photosynthetic apparatus. The expression of cold-induced genes, which are not controlled by Hik33, does not depend on the membrane fluidity or light. Thus, membrane fluidity determines the temperature dependence of the expression of cold-induced genes that are under control of the Hik33, which might be the sensor of changes in the membrane fluidity. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: from Natural to Artificial. (C) 2011 Elsevier B.V. All rights reserved.
引用
收藏
页码:1352 / 1359
页数:8
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