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. 1992 Mar;174(6):1869–1874. doi: 10.1128/jb.174.6.1869-1874.1992

Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutants.

C Ohtaka 1, H Nakamura 1, H Ishikawa 1
PMCID: PMC205790  PMID: 1347769

Abstract

An intracellular symbiont harbored by the aphid bacteriocyte, a specialized fat body cell, synthesizes in vivo substantially only one protein, symbionin, which is a member of the chaperonin-60 family of molecular chaperones. Nucleotide sequence determination of the symbionin region of the endosymbiont genome revealed that it contains the two-cistron operon sym. Just like the Escherichia coli groE operon, the sym operon was dually led by a heat shock and an ordinary promoter sequence. According to the nucleotide sequence, symbionin was 85.5% identical to GroEL of E. coli at the amino acid sequence level. SymS, another protein encoded in the sym operon, which is a member of chaperonin-10, was 79.6% identical to GroES. Complementation experiments with E. coli groE mutants showed that the chaperonin-10 and chaperonin-60 genes from the endosymbiont are expressed in E. coli and that they can function as molecular chaperones together with endogenous GroEL and GroES, respectively.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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