SSA3/YBL075C Literature Guide Help

Other names published for SSA3: YG106, Hsp70 family ATPase SSA3, YBL075C

SSA3 - Mutants/Phenotypes (26)

ReferenceOther Genes Addressed
Lancaster DL, et al.  (2013) Chaperone proteins select and maintain [PIN+] prion conformations in Saccharomyces cerevisiae. J Biol Chem 288(2):1266-76
Eliyahu E, et al.  (2012) The protein chaperone Ssa1 affects mRNA localization to the mitochondria. FEBS Lett 586(1):64-9
Saibil HR, et al.  (2012) Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures. Proc Natl Acad Sci U S A 109(37):14906-11
Winkler J, et al.  (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198(3):387-404
Bell SL, et al.  (2011) Expression of a Malarial Hsp70 Improves Defects in Chaperone-Dependent Activities in ssa1 Mutant Yeast. PLoS One 6(5):e20047
Fang NN, et al.  (2011) Hul5 HECT ubiquitin ligase plays a major role in the ubiquitylation and turnover of cytosolic misfolded proteins. Nat Cell Biol 13(11):1344-52
Jaiswal H, et al.  (2011) The chaperone network connected to human ribosome-associated complex. Mol Cell Biol 31(6):1160-73
Newnam GP, et al.  (2011) Destabilization and recovery of a yeast prion after mild heat shock. J Mol Biol 408(3):432-48
Juretschke J, et al.  (2010) The Hsp70 chaperone Ssa1 is essential for catabolite induced degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase. Biochem Biophys Res Commun 397(3):447-52
Ran F, et al.  (2010) Hsp90 cochaperone Aha1 is a negative regulator of the Saccharomyces MAL activator and acts early in the chaperone activation pathway. J Biol Chem 285(18):13850-62
Gong Y, et al.  (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5:275
Sharma D, et al.  (2009) Function of SSA subfamily of Hsp70 within and across species varies widely in complementing Saccharomyces cerevisiae cell growth and prion propagation. PLoS One 4(8):e6644
Wang RY, et al.  (2009) A temperature sensitive mutant of heat shock protein 70 reveals an essential role during the early steps of tombusvirus replication. Virology 394(1):28-38
Han S, et al.  (2007) Cytoplasmic Hsp70 promotes ubiquitination for endoplasmic reticulum-associated degradation of a misfolded mutant of the yeast plasma membrane ATPase, PMA1. J Biol Chem 282(36):26140-9
Park SH, et al.  (2007) The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system. Mol Biol Cell 18(1):153-65
Allen KD, et al.  (2005) Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]. Genetics 169(3):1227-42
Flower TR, et al.  (2005) Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease. J Mol Biol 351(5):1081-100
Schwock J, et al.  (2004) Interaction of 6-phosphofructokinase with cytosolic proteins of Saccharomyces cerevisiae. Yeast 21(6):483-94
Taxis C, et al.  (2003) Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J Biol Chem 278(38):35903-13
Lutz W, et al.  (2001) The role of heat shock protein 70 in vitamin D receptor function. Biochem Biophys Res Commun 282(5):1211-9
Zhang Y, et al.  (2001) Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Mol Biol Cell 12(5):1303-14
Schmidt PJ, et al.  (2000) Copper activation of superoxide dismutase 1 (SOD1) in vivo. Role for protein-protein interactions with the copper chaperone for SOD1. J Biol Chem 275(43):33771-6
Paz I, et al.  (1999) Monitoring dynamics of gene expression in yeast during stationary phase. Gene 236(1):33-42
Becker J, et al.  (1996) Functional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo. Mol Cell Biol 16(8):4378-86
Vogel JL, et al.  (1995) Heat-shock proteins Hsp104 and Hsp70 reactivate mRNA splicing after heat inactivation. Curr Biol 5(3):306-17
Sanchez Y, et al.  (1993) Genetic evidence for a functional relationship between Hsp104 and Hsp70. J Bacteriol 175(20):6484-91