SIS1/YNL007C Literature Guide Help

Other names published for SIS1: YNL007C

SIS1 - Protein Sequence Features (22)

ReferenceOther Genes Addressed
Hines JK, et al.  (2011) Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements. Prion 5(4):238-44
Hines JK, et al.  (2011) [SWI], the Prion Formed by the Chromatin Remodeling Factor Swi1, Is Highly Sensitive to Alterations in Hsp70 Chaperone System Activity. PLoS Genet 7(2):e1001309
Shorter J  (2011) The Mammalian disaggregase machinery: hsp110 synergizes with hsp70 and hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS One 6(10):e26319
Silva JC, et al.  (2011) Central domain deletions affect the SAXS solution structure and function of Yeast Hsp40 proteins Sis1 and Ydj1. BMC Struct Biol 11(1):40
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
Sharma D, et al.  (2009) Curing of Yeast [URE3] Prion by the Hsp40 Cochaperone Ydj1p Is Mediated by Hsp70. Genetics 181(1):129-37
Douglas PM, et al.  (2008) Chaperone-dependent amyloid assembly protects cells from prion toxicity. Proc Natl Acad Sci U S A 105(20):7206-11
Ramos CH, et al.  (2008) Conserved central domains control the quaternary structure of type I and type II Hsp40 molecular chaperones. J Mol Biol 383(1):155-66
Aron R, et al.  (2007) J-protein co-chaperone Sis1 required for generation of [RNQ+] seeds necessary for prion propagation. EMBO J 26(16):3794-803
Li J, et al.  (2006) Crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex. Biochem J 398(3):353-60
Aron R, et al.  (2005) In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae. Genetics 169(4):1873-82
Mah AS, et al.  (2005) Substrate specificity analysis of protein kinase complex Dbf2-Mob1 by peptide library and proteome array screening. BMC Biochem 6():22
Fan CY, et al.  (2004) Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol Biol Cell 15(2):761-73
Lopez N, et al.  (2003) Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+]. Mol Biol Cell 14(3):1172-81
Qian X, et al.  (2002) Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1. Biochem J 361(Pt 1):27-34
Johnson JL and Craig EA  (2001) An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae. J Cell Biol 152(4):851-6
Qian X, et al.  (2001) Cloning, expression, purification and preliminary X-ray crystallographic studies of yeast Hsp40 Sis1 complexed with Hsp70 Ssa1 C-terminal lid domain. Acta Crystallogr D Biol Crystallogr 57(Pt 5):748-50
Sondheimer N, et al.  (2001) The role of Sis1 in the maintenance of the [RNQ+] prion. EMBO J 20(10):2435-42
Sha B and Cyr D  (1999) Purification, crystallization and preliminary X-ray crystallographic studies of S. cerevisiae Hsp40 Sis1. Acta Crystallogr D Biol Crystallogr 55(Pt 6):1234-6
Yan W and Craig EA  (1999) The glycine-phenylalanine-rich region determines the specificity of the yeast Hsp40 Sis1. Mol Cell Biol 19(11):7751-8
Lu Z and Cyr DM  (1998) Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J Biol Chem 273(43):27824-30
Luke MM, et al.  (1991) Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins. J Cell Biol 114(4):623-38