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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Veröffentlicht in: | Gene 1990, Vol.94 (2), p.181-187 |
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Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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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ISSN: | 0378-1119 1879-0038 |
DOI: | 10.1016/0378-1119(90)90385-5 |