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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Dates
Type | When |
---|---|
Created | 8 years, 9 months ago (Nov. 4, 2016, 3:52 p.m.) |
Deposited | 4 years, 1 month ago (July 29, 2021, 1:49 p.m.) |
Indexed | 1 month ago (July 24, 2025, 7:14 a.m.) |
Issued | 33 years, 5 months ago (March 1, 1992) |
Published | 33 years, 5 months ago (March 1, 1992) |
Published Print | 33 years, 5 months ago (March 1, 1992) |
@article{Ohtaka_1992, title={Structures of chaperonins from an intracellular symbiont and their functional expression in Escherichia coli groE mutants}, volume={174}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.174.6.1869-1874.1992}, DOI={10.1128/jb.174.6.1869-1874.1992}, number={6}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Ohtaka, C and Nakamura, H and Ishikawa, H}, year={1992}, month=mar, pages={1869–1874} }