细菌热休克蛋白ClpB/HSP100的截短形式有助于蓝藻聚球藻属PCC 7942菌株耐热性的形成。
The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942.
作者信息
Clarke A K, Eriksson M J
机构信息
Umeå Plant Sciences Centre, Department of Plant Physiology, University of Umeâ, Umeâ S-901 87, Sweden.
出版信息
J Bacteriol. 2000 Dec;182(24):7092-6. doi: 10.1128/JB.182.24.7092-7096.2000.
Abstract
ClpB is a highly conserved heat shock protein that is essential for thermotolerance in bacteria and eukaryotes. One distinctive feature of all bacterial clpB genes is the dual translation of a truncated 79-kDa form (ClpB-79) in addition to the full-length 93-kDa protein (ClpB-93). To investigate the currently unknown function of ClpB-79, we have examined the ability of the two different-sized ClpB homologues from the cyanobacterium Synechococcus sp. strain PCC 7942 to confer thermotolerance. We show that the ClpB-79 form has the same capacity as ClpB-93 to confer thermotolerance and that the ClpB-79 protein contributes ca. one-third of the total thermotolerance developed in wild-type Synechococcus, the first in vivo demonstration of a functional role for ClpB-79 in bacteria.
摘要
ClpB是一种高度保守的热休克蛋白，对细菌和真核生物的耐热性至关重要。所有细菌clpB基因的一个显著特征是，除了全长93 kDa的蛋白质（ClpB-93）外，还会双重翻译出截短的79 kDa形式（ClpB-79）。为了研究目前未知的ClpB-79的功能，我们检测了来自蓝藻聚球藻属PCC 7942菌株的两种不同大小的ClpB同源物赋予耐热性的能力。我们发现，ClpB-79形式与ClpB-93具有相同的赋予耐热性的能力，并且ClpB-79蛋白对野生型聚球藻产生的总耐热性贡献约三分之一，这是首次在体内证明ClpB-79在细菌中的功能作用。
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