Unique composition of plastid chaperonin-60: α and β polypeptide-encoding genes are highly divergent
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 (p60 cpn-60 ). In contrast, preparations of purified plastid Cpn-60 contain approximately equal qu...
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Published in | Gene Vol. 94; no. 2; pp. 181 - 187 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Lausanne
Elsevier B.V
1990
Amsterdam Elsevier New York, NY |
Subjects | |
Online Access | Get full text |
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Summary: | 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 (p60
cpn-60
). In contrast, preparations of purified plastid Cpn-60 contain approximately equal quantities of two polypeptides, p60
cpn-60α
and p60
cpn-60β
, with slightly different electrophoretic mobilities. We have isolated cDNA clones encoding plastid p60
cpn-60α
and p60
cpn-60β
polypeptides from
Brassica napus and
Arabidopsis thaliana. The unexpected degree of sequence divergence observed between p60
cpn-60α
and p60
cpn-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 p60
cpn-60
sequences which resembles the p10
cpn-10
sequences. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0378-1119 1879-0038 |
DOI: | 10.1016/0378-1119(90)90385-5 |