W L Kelley
Affiliation: University of Geneva
- The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperoneW L Kelley
Departement de Biochimie Medicale, Centre Medical Universitaire, Universite de Geneve, Geneva, Switzerland
Proc Natl Acad Sci U S A 94:3679-84. 1997..This finding has implications for the regulation of DNA tumor virus T antigens by molecular chaperones...
- Positive control of the two-component RcsC/B signal transduction network by DjlA: a member of the DnaJ family of molecular chaperones in Escherichia coliW L Kelley
Departement de Biochimie Medicale, Universite de Geneve, Switzerland
Mol Microbiol 25:913-31. 1997....
- The J-domain family and the recruitment of chaperone powerW L Kelley
Dept de Biochimie Médicale, Centre Medical Universitaire, Universite de Geneve, Switzerland
Trends Biochem Sci 23:222-7. 1998..J-domain proteins participate in complex biological processes, such as cell-cycle control by DNA tumor viruses, regulation of protein kinases and exocytosis...
- Molecular chaperones: How J domains turn on Hsp70sW L Kelley
Departement de Biochimie Medicale, CMU Université de Genève, 1 rue Michel Servet, 1211 Geneve 4, Switzerland
Curr Biol 9:R305-8. 1999..They are assisted in this role by their Hsp40 partners, and recent studies have shed new light on how the 'J domains' of these 'cochaperones' activate substrate binding by Hsp70 molecules...
- Structure-function analyses of the Ssc1p, Mdj1p, and Mge1p Saccharomyces cerevisiae mitochondrial proteins in Escherichia coliO Deloche
, , Geneva, Switzerland
J Bacteriol 179:6066-75. 1997..coli. We were unable to demonstrate any functional complementation by Ssc1p, even when coexpressed with its Mdj1p cochaperone in E. coli...
- The djlA gene acts synergistically with dnaJ in promoting Escherichia coli growthP Genevaux
Departement de Biochimie Medicale, Centre Medical Universitaire, Universite de Geneve, 1211 Geneve 4, Switzerland
J Bacteriol 183:5747-50. 2001..This essentiality depended upon the J domain of DjlA but not upon the normal membrane location of DjlA...
- DjlA is a third DnaK co-chaperone of Escherichia coli, and DjlA-mediated induction of colanic acid capsule requires DjlA-DnaK interactionP Genevaux
Departement de Biochimie Medicale, Centre Medical Universitaire, Universite de Geneve, 1, rue Michel Servet, 1211 Geneve 4, Switzerland
J Biol Chem 276:7906-12. 2001..Collectively, these results demonstrate that DjlA is a co-chaperone for DnaK and that this chaperone-co-chaperone pair is implicated directly, or indirectly, in the regulation of colanic acid capsule...
- Replication terminator protein of Escherichia coli is a transcriptional repressor of its own synthesisS Natarajan
Department of Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710
Proc Natl Acad Sci U S A 88:3867-71. 1991..Therefore, Ter protein can serve as a transcriptional repressor of its own synthesis by preventing RNA polymerase from binding to the tus promoter when both proteins are present in the cell milieu...