Genomes and Genes
Gene Symbol: TAH1
Species: Saccharomyces cerevisiae S288c
- The Hsp90 chaperone controls the biogenesis of L7Ae RNPs through conserved machinerySéverine Boulon
Institute of Molecular Genetics of Montpellier, Centre National de la Recherche Scientifique, Unite Mixte de Recherche 5535, Montpellier Cedex 5, France
J Cell Biol 180:579-95. 2008..the AAA + adenosine triphosphatases hRvb1 and hRvb2 and with the Hsp90 chaperone through two conserved adaptors, Tah1/hSpagh and Pih1...
- Chaperone ligand-discrimination by the TPR-domain protein Tah1Stefan H Millson
Department of Molecular Biology and Biotechnology, The University of Sheffield, Firth Court, Western Bank, Sheffield S10 2TN, UK
Biochem J 413:261-8. 2008b>Tah1 [TPR (tetratricopeptide repeat)-containing protein associated with Hsp (heat-shock protein) 90] has been identified as a TPR-domain protein...
- The Pih1-Tah1 cochaperone complex inhibits Hsp90 molecular chaperone ATPase activityKelvin Eckert
Laboratoire d Enzymologie et Biochimie Structurales, CNRS, 91198 Gif sur Yvette, France
J Biol Chem 285:31304-12. 2010..TPR (TetratricoPeptide Repeat)-containing protein associated with Hsp90 (Tah1) and protein interacting with Hsp90 (Pih1) have been identified in Saccharomyces cerevisiae as two Hsp90 ..
- Structure of minimal tetratricopeptide repeat domain protein Tah1 reveals mechanism of its interaction with Pih1 and Hsp90Beatriz Jimenez
Structural Biochemistry Laboratory, Medicinal Chemistry Department, Centro de Investigacion Principe Felipe, E 46012 Valencia, Spain
J Biol Chem 287:5698-709. 2012b>Tah1 and Pih1 are novel Hsp90 interactors. Tah1 acts as a cofactor of Hsp90 to stabilize Pih1...
- The stability of the small nucleolar ribonucleoprotein (snoRNP) assembly protein Pih1 in Saccharomyces cerevisiae is modulated by its C terminusAlexandr Paci
Department of Biological Sciences, University of Toronto, Toronto, Ontario M1C 1A4, Canada
J Biol Chem 287:43205-14. 2012..complex that, in yeast Saccharomyces cerevisiae, also contains the helicases Rvb1, Rvb2, and the Hsp90 cofactor Tah1. Pih1 and the R2TP complex are required for the box C/D small nucleolar ribonucleoprotein (snoRNP) assembly and ..
- High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complexRégis Back
Ingénierie Moléculaire et Physiopathologie Articulaire IMoPA, UMR 7365 Université de Lorraine CNRS, Biopôle de l Université de Lorraine, Campus Biologie Santé, 9 Avenue de la Forêt de Haye, BP 184, 54505 Vandœuvre Lès Nancy, France
Structure 21:1834-47. 2013..This complex includes the proteins Tah1, Pih1, Rvb1, and Rvb2. Tah1 bridges Hsp90 to R2TP...
- Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1Mohinder Pal
MRC Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9RQ, UK
Structure 22:805-18. 2014..complexes depends on the TTT (Tel2-Tti1-Tti2), and R2TP complexes-consisting of the AAA-ATPases Rvb1 and Rvb2, Tah1 (Spagh/RPAP3 in metazoa), and Pih1 (Pih1D1 in humans)-that together provide the connection to Hsp90...
- (1)H, (15)N and (13)C resonance assignments of the yeast Pih1 and Tah1 C-terminal domains complexXavier Manival
Ingénierie Moléculaire et Physiopathologie Articulaire IMoPA, UMR 7365 CNRS, Université de Lorraine, Biopôle de l Université de Lorraine, Campus Biologie Santé, 9 Avenue de la Forêt de Haye, CS 50184, 54505, Vandœuvre lès Nancy, France
Biomol NMR Assign 9:71-3. 2015We report the nearly complete (1)H, (15)N and (13)C resonance assignment of the complex formed by the C-terminal domains of Pih1 and Tah1 from S. cerevisiae and evidence the folding ability of Tah1 under complex formation.
- Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperonesJill L Johnson
Department of Biological Sciences, University of Idaho, P O Box 443051, Moscow, ID, 83844 3051, USA
Curr Genet 60:265-76. 2014..This provides new evidence that co-chaperones selectively compete for binding to subpopulations of cellular Hsp90 and suggest that changes in the relative levels of co-chaperones may have dramatic effects on Hsp90 function...
- Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interactionBenjamin Rothé
Ingénierie Moléculaire et Physiopathologie Articulaire IMoPA, UMR 7365 CNRS Université de Lorraine, Biopôle, Campus Biologie Santé, 9 Avenue de la Forêt de Haye, CS 50184, 54505 Vandœuvre Lès Nancy, France
Nucleic Acids Res 42:10731-47. 2014..Our biochemical data show that C/D snoRNAs and the core protein Nop58 can interact with the purified Snu13p-Rsa1p-Hit1p heterotrimer. ..
- Tah1 helix-swap dimerization prevents mixed Hsp90 co-chaperone complexesRhodri M L Morgan
Genome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer, Brighton BN1 9RQ, England
Acta Crystallogr D Biol Crystallogr 71:1197-206. 2015Specific co-chaperone adaptors facilitate the recruitment of client proteins to the Hsp90 system. Tah1 binds the C-terminal conserved MEEVD motif of Hsp90, thus linking an eclectic set of client proteins to the R2TP complex for their ..
- Structure/Function Analysis of Protein-Protein Interactions Developed by the Yeast Pih1 Platform Protein and Its Partners in Box C/D snoRNP AssemblyMarc Quinternet
FR 3209 CNRS Université de Lorraine, Bioingénierie Moléculaire, Cellulaire et Thérapeutique, Biopôle, Campus Biologie Santé, CS 50184, 54505 Vandœuvre lès Nancy Cedex, France
J Mol Biol 427:2816-39. 2015..Our data suggest that these two interactions are mutually exclusive. The implication of this finding for box C/D small nucleolar ribonucleoparticle assembly is discussed. ..
- Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiaeDavid L Lancaster
Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada
J Biol Chem 288:1266-76. 2013..Together, our results demonstrate a role for chaperones in regulating the prion variant complement of a cell...
- Mutations in SID2, a novel gene in Saccharomyces cerevisiae, cause synthetic lethality with sic1 deletion and may cause a defect during S phaseM D Jacobson
The Rockefeller University, New York, New York 10021, USA
Genetics 159:17-33. 2001..Consistent with this hypothesis, sid2-1 rad9 cells are dead or very slow growing even when SIC1 is expressed...
- Alternative oligomeric states of the yeast Rvb1/Rvb2 complex induced by histidine tagsKevin L Y Cheung
Department of Biochemistry and Biomedical Sciences and M G DeGroote Institute for Infectious Diseases Research, Health Sciences Center, McMaster University, 1200 Main Street West, Hamilton, Ontario, Canada L8N 3Z5
J Mol Biol 404:478-92. 2010..These results demonstrate that some of the differences between the reported structures are caused by histidine tags and imply that further studies on the purified proteins should be carried out using untagged constructs...