Identification of a chaperonin-10 homologue in plant mitochondria.
Chaperonin-60 and chaperonin-10 form stable binary complexes in the presence of ATP. This phenomenon has been used as the basis for the identification of a chaperonin-10 homologue in potato (Solanum tuberosum L.) mitochondria. ATP-dependent binary complexes formed between chaperonin-60 and chaperonin-10 in potato mitochondrial extracts were isolated by affinity chromatography on a column of immobilised chaperonin-60 antibodies. Partial amino acid sequence analysis of the chaperonin-10 protein indicates that it is related in primary structure to rat mitochondrial chaperonin-10.
Burt
W J
WJ
Department of Plant Sciences, University of Oxford, UK.
Leaver
C J
CJ
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D018835:Chaperonin 10; D018834:Chaperonin 60; D002851:Chromatography, High Pressure Liquid; D006360:Heat-Shock Proteins / Q000032:analysis* / Q000378:metabolism; D008928:Mitochondria / Q000737:chemistry*; D008969:Molecular Sequence Data; D010944:Plants / Q000648:ultrastructure*; D051381:Rats; D017386:Sequence Homology, Amino Acid; D011198:Solanum tuberosum
D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D000255:Adenosine Triphosphate