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Farnesylation of Ydj1 Is Required for In Vivo Interaction with Hsp90 Client Proteins
- Source :
- Molecular Biology of the Cell. 19:5249-5258
- Publication Year :
- 2008
- Publisher :
- American Society for Cell Biology (ASCB), 2008.
-
Abstract
- Ydj1 of Saccharomyces cerevisiae is an abundant cytosolic Hsp40, or J-type, molecular chaperone. Ydj1 cooperates with Hsp70 of the Ssa family in the translocation of preproteins to the ER and mitochondria and in the maturation of Hsp90 client proteins. The substrate-binding domain of Ydj1 directly interacts with steroid receptors and is required for the activity of diverse Hsp90-dependent client proteins. However, the effect of Ydj1 alteration on client interaction was unknown. We analyzed the in vivo interaction of Ydj1 with the protein kinase Ste11 and the glucocorticoid receptor. Amino acid alterations in the proposed client-binding domain or zinc-binding domain had minor effects on the physical interaction of Ydj1 with both clients. However, alteration of the carboxy-terminal farnesylation signal disrupted the functional and physical interaction of Ydj1 and Hsp90 with both clients. Similar effects were observed upon deletion of RAM1, which encodes one of the subunits of yeast farnesyltransferase. Our results indicate that farnesylation is a major factor contributing to the specific requirement for Ydj1 in promoting proper regulation and activation of diverse Hsp90 clients.
- Subjects :
- Models, Molecular
Saccharomyces cerevisiae Proteins
Recombinant Fusion Proteins
Protein subunit
Farnesyltransferase
Saccharomyces cerevisiae
medicine.disease_cause
Receptors, Glucocorticoid
Prenylation
Transferases
medicine
Animals
Humans
HSP90 Heat-Shock Proteins
Protein kinase A
Molecular Biology
Mutation
MAP kinase kinase kinase
biology
Articles
Cell Biology
HSP40 Heat-Shock Proteins
MAP Kinase Kinase Kinases
biology.organism_classification
Hsp90
Protein Structure, Tertiary
Rats
Protein Subunits
Biochemistry
biology.protein
Gene Deletion
Subjects
Details
- ISSN :
- 19394586 and 10591524
- Volume :
- 19
- Database :
- OpenAIRE
- Journal :
- Molecular Biology of the Cell
- Accession number :
- edsair.doi.dedup.....4a01887136872eb879a5bc02b706b324