Site groS
- Name: groS
- Type: Gene
- Synonyms
b4142 MG1655 locus tag groES mopB 90 map - Mnemonic: growth of phage
- Left End Point: 94.16
- Right End Point: 94.17
- Products:
Hsp60, chaperone subunit GroES - Direction: >
- Properties:
Property Comment heat shock regulon NULL - Priority: 1
- 1 Alleles of This Gene
groS791-YFP(::cat) - External Database Links:
Host Site Page Links EcoGene.org EG10600 EcoliWiki groS - Comment:
- Selectable phenotype. Phage LAM + phage 434, phage T4 resistance.
- References:
- Georgopoulos, C., R.W. Hendrix, C. Kaiser 1972. Role of the host cell in bacteriophage morphogenesis: effects of a bacterial mutation on T4 head assembly. Nature New Biol. 239:38-41
- Neidhardt, F.C., T.A. Phillips, R.A. VanBogelen, M. W. Smith, Y. Georgalis, A.R. Subramanian 1981. Identity of the B56.5 protein, the A-protein, and the groE gene product of Escherichia coli. J.Bacteriol. 145:513-520
- Tilly, K., H. Murialdo, C. Georgopoulos 1981. Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc.Natl.Acad.Sci.USA 78:1629-1633
- Laine, P.S., R.R. Meyer 1992. Interaction of the heat shock protein GroEL of Escherichia coli with single-stranded DNA-binding protein: suppression of ssb-113 by groEL46. J.Bacteriol. 174:3204-3211
- Donnelly, C.E., G.C. Walker 1992. Coexpression of UmuD' with UmuC suppresses the UV mutagenesis deficiency of groE mutants. J.Bacteriol. 174:3133-3139
- Zondlo, J., K.E. Fisher, Z. Lin, K.R. Ducote, E. Eisenstein 1995. Monomer-heptamer equilibrium of the Escherichia coli chaperonin GroES. Biochemistry 34:10334-0
- Kandror, O., M. Sherman, M. Rhode, A.L. Goldberg 1995. Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. EMBO J. 14:6021-6027
- Legname, G., P. Buono, G. Fossati, N. Monzini, P. Mascagni, D. Modena, F. Marcucci 1996. Evidence for GroES acting as a transcriptional regulator. Biochem.Biophys.Res.Commun. 229:412-418
- Martin, J. 1998. Role of the GroEL chaperonin intermediate domain in coupling ATP hydrolysis to polypeptide release. J.Biol.Chem. 273:7351-7357