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小热激蛋白在蓝藻聚球藻属嗜热栖热菌PCC 7942的htpG缺失突变体中的组成型表达。

Constitutive expression of small heat shock protein in an htpG disruptant of the Cyanobacterium Synechococcus sp. PCC 7942.

作者信息

Kojima Kouji, Nakamoto Hitoshi

机构信息

Department of Biochemistry and Molecular Biology, Saitama University, Saitama, 338-8570, Japan.

出版信息

Curr Microbiol. 2005 May;50(5):272-6. doi: 10.1007/s00284-005-4486-9. Epub 2005 Apr 11.

Abstract

In cyanobacteria, a disruptant of hspA encoding a small heat shock protein homologue, shows decreased cell growth rates at moderately high temperatures, and loss of both basal and acquired thermo-tolerances, which resemble the phenotype of an htpG disruptant. In vitro studies have shown that both small heat shock protein and Hsp90 can bind and keep non-native proteins in a refolding-competent state under denaturing conditions. The aim of the present study is to elucidate whether constitutive expression of HspA can functionally replace HtpG, a prokaryotic homolog of Hsp90, in the cyanobacterium Synechococcus sp. PCC 7942. HspA did not improve the viability of the htpG disruptant at a lethal temperature, although it did that of the wild type. It did not improve an iron-starved phenotype of the mutant under normal growth conditions, a novel phenotype found in the present study. These results suggest that cellular function of HtpG may differ significantly from that of HspA.

摘要

在蓝细菌中,编码小热激蛋白同源物的hspA的破坏突变体在适度高温下细胞生长速率降低,并且丧失了基础耐热性和获得性耐热性,这与htpG破坏突变体的表型相似。体外研究表明,小热激蛋白和Hsp90在变性条件下都能结合并使非天然蛋白质保持在可重折叠的状态。本研究的目的是阐明HspA的组成型表达是否能在集胞藻属PCC 7942蓝细菌中功能性替代Hsp90的原核同源物HtpG。HspA在致死温度下并未提高htpG破坏突变体的活力,尽管它提高了野生型的活力。在正常生长条件下,它也未改善本研究中发现的突变体的铁饥饿表型。这些结果表明,HtpG的细胞功能可能与HspA的细胞功能有显著差异。

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