The unusual mycobacterial chaperonins: evidence for in vivo oligomerization and specialization of function.
作者： MingQi Fan , Tara Rao , Elsa Zacco , M. Tabish Ahmed , Anshuman Shukla
DOI: 10.1111/J.1365-2958.2012.08150.X
关键词:
摘要: The pathogen Mycobacterium tuberculosis expresses two chaperonins, one (Cpn60.1) dispensable and (Cpn60.2) essential. These proteins have been reported not to form oligomers despite the fact that oligomerization of chaperonins is regarded as essential for their function. We show here Cpn60.2 homologue from smegmatis also fails oligomerize under standard conditions. However, we both organisms can replace groEL gene Escherichia coli, they function with E. coli GroES cochaperonin, well cognate cochaperonin proteins, strongly implying in vivo. Cpn60.1 but complement loss M. cpn60.1 gene. investigated using analytical ultracentrifugation mass spectroscopy. Both monomers conditions, higher order presence kosmotropes ADP or ATP. Under these ATPase activity significantly enhanced. conclude mycobacterial while unstable compared many other bacterial do act vivo, there has specialization following duplication.
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