SSA1/YAL005C Literature Guide Help

Other names published for SSA1: YG100, Hsp70 family ATPase SSA1, YAL005C

SSA1 - Genetic Interactions (60)

ReferenceOther Genes Addressed
Eliyahu E, et al.  (2012) The protein chaperone Ssa1 affects mRNA localization to the mitochondria. FEBS Lett 586(1):64-9
Kiktev DA, et al.  (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70
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
Kirkland PA, et al.  (2011) Functions of yeast Hsp40 chaperone Sis1p dispensable for prion propagation but important for prion curing and protection from prion toxicity. Genetics 188(3):565-77
Sanada M, et al.  (2011) Inhibition of heat tolerance and nuclear import of gts1p by ssa1p and ssa2p. Biosci Biotechnol Biochem 75(2):323-30
Heck JW, et al.  (2010) Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc Natl Acad Sci U S A 107(3):1106-11
Moosavi B, et al.  (2010) Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation. Yeast 27(3):167-79
Nillegoda NB, et al.  (2010) Ubr1 and ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins. Mol Biol Cell 21(13):2102-16
Reidy M and Masison DC  (2010) Sti1 Regulation of Hsp70 and Hsp90 Is Critical for Curing of Saccharomyces cerevisiae [PSI+] Prions by Hsp104. Mol Cell Biol 30(14):3542-52
Weeks SA, et al.  (2010) A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication. J Virol 84(1):330-9
Wang RY, et al.  (2009) A key role for heat shock protein 70 in the localization and insertion of tombusvirus replication proteins to intracellular membranes. J Virol 83(7):3276-87
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
Bandhakavi S, et al.  (2008) Hsf1 Activation Inhibits Rapamycin Resistance and TOR Signaling in Yeast Revealed by Combined Proteomic and Genetic Analysis. PLoS ONE 3(2):e1598
Sadlish H, et al.  (2008) Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE 3(3):e1763
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
Shahi P, et al.  (2007) Negative transcriptional regulation of multidrug resistance gene expression by an Hsp70 protein. J Biol Chem 282(37):26822-31
Wright CM, et al.  (2007) The Hsp40 molecular chaperone Ydj1p, along with the protein kinase C pathway, affects cell-wall integrity in the yeast Saccharomyces cerevisiae. Genetics 175(4):1649-64
Borchsenius AS, et al.  (2006) Prion variant maintained only at high levels of the Hsp104 disaggregase. Curr Genet 49(1):21-9
Dehay B and Bertolotti A  (2006) Critical Role of the Proline-rich Region in Huntingtin for Aggregation and Cytotoxicity in Yeast. J Biol Chem 281(47):35608-15
Hung GC and Masison DC  (2006) N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression. Genetics 173(2):611-20
Matsumoto R, et al.  (2006) Search for novel stress-responsive protein components using a yeast mutant lacking two cytosolic Hsp70 genes, SSA1 and SSA2. Mol Cells 21(3):381-8
Tabuchi M, et al.  (2006) The phosphatidylinositol 4,5-biphosphate and TORC2 binding proteins Slm1 and Slm2 function in sphingolipid regulation. Mol Cell Biol 26(15):5861-75
Matsumoto R, et al.  (2005) The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae. BMC Genomics 6():141
Otto H, et al.  (2005) The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. Proc Natl Acad Sci U S A 102(29):10064-9
Yam AY, et al.  (2005) Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. J Biol Chem 280(50):41252-61
Huyer G, et al.  (2004) Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J Biol Chem 279(37):38369-78
Jones G, et al.  (2004) Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding. Mol Cell Biol 24(9):3928-37
Roberts BT, et al.  (2004) [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast. Yeast 21(2):107-17
Tong AH, et al.  (2004) Global mapping of the yeast genetic interaction network. Science 303(5659):808-13