UNIQUE COMPOSITION OF PLASTID CHAPERONIN-60 - ALPHA-POLYPEPTIDE-ENCODING AND BETA-POLYPEPTIDE-ENCODING GENES ARE HIGHLY DIVERGENT

被引：95

作者：

MARTEL, R ^{[1
]}

CLONEY, LP ^{[1
]}

PELCHER, LE ^{[1
]}

HEMMINGSEN, SM ^{[1
]}

机构：

[1] NATL RES COUNCIL CANADA,INST PLANT BIOTECHNOL,SASKATOON S7N 0W9,SASKATCHEWAN,CANADA

来源：

GENE | 1990年 / 94卷 / 02期

关键词：

Arabidopsis thaliana; ATPase; Brassica napus; heat shock; Molecular chaperones; recombinant DNA;

D O I：

10.1016/0378-1119(90)90385-5

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

Molecular chaperones of the chaperonin family occur in prokaryotes and in plastids and mitochondria. Prokaryotic and mitochondrial chaperonin-60 oligomers (Cpn-60) are composed of a single subunit type (p60cpn-60). In contrast, preparations of purified plastid Cpn-60 contain approximately equal quantities of two polypeptides, p60cpn-60α and p60cpn-60β, with slightly different electrophoretic mobilities. We have isolated cDNA clones encoding plastid p60cpn-60α and p60cpn-60β polypeptides from Brassica napus and Arabidopsis thaliana. The unexpected degree of sequence divergence observed between p60cpn-60α and p60cpn-60β raises questions concerning the structure of the oligomer and the functions of these polypeptides. We have also found an amino acid sequence motif within all p60cpn-60 sequences which resembles the p10cpn-10 sequences. © 1990.

引用

页码：181 / 187

页数：7

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