UNIQUE COMPOSITION OF PLASTID CHAPERONIN-60 - ALPHA-POLYPEPTIDE-ENCODING AND BETA-POLYPEPTIDE-ENCODING GENES ARE HIGHLY DIVERGENT
UNIQUE COMPOSITION OF PLASTID CHAPERONIN-60 - ALPHA-POLYPEPTIDE-ENCODING AND BETA-POLYPEPTIDE-ENCODING GENES ARE HIGHLY DIVERGENT
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DOI:
10.1016/0378-1119(90)90385-5
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发表时间:
1990-10-15
期刊:
影响因子:
3.5
通讯作者:
HEMMINGSEN, SM
中科院分区:
文献类型:
--
作者:
MARTEL, R;CLONEY, LP;HEMMINGSEN, SM
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-60.alpha. and p60cpn-60.beta., with slightly different electrophoretic mobilities. We have isolated cDNA clones encoding plastid p60cpn-60.alpha. and p60cpn-60.beta. polypeptides from Brassica napus and Arabidopsis thaliana. The unexpected degree of sequence divergence observed between p60cpn-60.alpha. and p60cpn-60.beta. 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.