Johnson R B, Fearon K, Mason T, Jindal S
Whitehead Institute for Biomedical Research, Cambridge, MA.
Gene. 1989 Dec 14;84(2):295-302. doi: 10.1016/0378-1119(89)90503-9.
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].
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]。
