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PMID:12071968

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Citation

Bochkareva, ES, Girshovich, AS and Bibi, E (2002) Identification and characterization of the Escherichia coli stress protein UP12, a putative in vivo substrate of GroEL. Eur. J. Biochem. 269:3032-40

Abstract

Many groups of proteins play important roles in the cell's response to various stresses. The molecular chaperone GroEL of Escherichia coli represents one such highly conserved family of stress proteins. We have observed that isolated GroEL complexes from stationary cultures contain various polypeptides that can be released from the chaperonin by GroES and/or ATP, and identified two such polypeptides as the proteins GatY and UP12. Whereas GatY had been isolated previously, as an in vivo substrate of GroEL, the isolation of UP12 in a complex with GroEL was intriguing, because based on sequence similarity it was suggested that UP12 might also be a functional stress protein. UP12 belongs to a family of universal stress proteins (UspA family), of which UspA itself, and three additional paralogues, have been characterized previously. Here we show that UP12 accumulates under various growth inhibitory conditions and induced by heat shock. Furthermore, unlike wild-type cells, a UP12 deletion mutant recovers slowly from late stationary growth conditions, and has a marked sensitivity to the toxic agent carbonyl cyanide m-chlorophenyl hydrazone (CCCP). Finally, coimmunoprecipitation experiments confirmed the initial observation that UP12 interacts with GroEL. Therefore, we suggest that UP12 may function as a universal stress protein, interaction of which with GroEL possibly ensures its proper folding state.

Links

PubMed

Keywords

Amino Acid Sequence; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Binding Sites; Carbon/deficiency; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology; Chaperonin 60/metabolism; Dinitrophenols/pharmacology; Escherichia coli/drug effects; Escherichia coli/metabolism; Escherichia coli Proteins/genetics; Escherichia coli Proteins/isolation & purification; Escherichia coli Proteins/metabolism; Heat-Shock Proteins/genetics; Heat-Shock Proteins/isolation & purification; Heat-Shock Proteins/metabolism; Hot Temperature; Molecular Sequence Data; Mutation; Peptides/genetics; Peptides/isolation & purification; Peptides/metabolism; Phosphates/deficiency; Sequence Homology, Amino Acid

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:CH60

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P39177

F

Seeded From UniProt

complete

ECOLI:USPG

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0A6F5

F

Seeded From UniProt

complete

ECOBW:C4ZW97

GO:0006950: response to stress

IDA: Inferred from Direct Assay:

P

See Fig. 4 and Fig. 5

complete



See also

References

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