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酵母伴侣蛋白HSP60基因的克隆与特性分析

Cloning and characterization of the yeast chaperonin HSP60 gene.

作者信息

Johnson R B, Fearon K, Mason T, Jindal S

机构信息

Whitehead Institute for Biomedical Research, Cambridge, MA.

出版信息

Gene. 1989 Dec 14;84(2):295-302. doi: 10.1016/0378-1119(89)90503-9.

Abstract

The heat-shock protein, HSP60, is abundant in prokaryotes and eukaryotes and is required in the assembly of specific proteins. We have cloned the Saccharomyces cerevisiae HSP60 gene from a lambda gt11 genomic library using monoclonal antibodies, have obtained its sequence, determined its transcription start point, and shown that it exists as a single copy. The predicted HSP60 contains a mitochondrial target sequence and exhibits striking amino acid sequence similarity to its counterparts in bacteria, plants, and humans. These data indicate a high level of evolutionary conservation and are consistent with the suggestion of evolutionarily conserved function [Hemmingsen et al., Nature 333 (1988), 330-334].

摘要

热休克蛋白HSP60在原核生物和真核生物中含量丰富,是特定蛋白质组装所必需的。我们利用单克隆抗体从λgt11基因组文库中克隆了酿酒酵母HSP60基因,获得了其序列,确定了其转录起始点,并表明它以单拷贝形式存在。预测的HSP60含有线粒体靶向序列,并且与其在细菌、植物和人类中的对应物表现出惊人的氨基酸序列相似性。这些数据表明了高度的进化保守性,并且与进化上保守功能的观点一致[亨明森等人,《自然》333(1988),330 - 334]。

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