YDJ1/YNL064C Literature Guide Help

Other names published for YDJ1: MAS5, HSP40, YNL064C

YDJ1 - Function/Process (83)

ReferenceOther Genes Addressed
Duennwald ML, et al.  (2012) Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans. PLoS Biol 10(6):e1001346
Ferrezuelo F, et al.  (2012) The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation. Nat Commun 3():1012
Gillies AT, et al.  (2012) Synthetic lethal interactions in yeast reveal functional roles of J protein co-chaperones. Mol Biosyst 8(11):2901-8
Nowicki L, et al.  (2012) Role of a conserved aspartic acid in nucleotide binding domain 1 (NBD1) of Hsp100 chaperones in their activities. Cell Stress Chaperones 17(3):361-73
Reidy M, et al.  (2012) Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics 192(1):185-93
Kryndushkin DS, et al.  (2011) Molecular chaperone Hsp104 can promote yeast prion generation. Genetics 188(2):339-48
Morell M, et al.  (2011) Linking amyloid protein aggregation and yeast survival. Mol Biosyst 7(4):1121-8
Moriel-Carretero M, et al.  (2011) Control of the function of the transcription and repair factor TFIIH by the action of the cochaperone Ydj1. Proc Natl Acad Sci U S A 108(37):15300-5
Sharma D and Masison DC  (2011) Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p. Proc Natl Acad Sci U S A 108(33):13665-70
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
Polier S, et al.  (2010) Interaction of the Hsp110 Molecular Chaperones from S. cerevisiae with Substrate Protein. J Mol Biol 401(5):696-707
Prasad R, et al.  (2010) A nucleus-based quality control mechanism for cytosolic proteins. Mol Biol Cell 21(13):2117-27
Abe F and Minegishi H  (2008) Global screening of genes essential for growth in high-pressure and cold environments: searching for basic adaptive strategies using a yeast deletion library. Genetics 178(2):851-72
Higurashi T, et al.  (2008) Specificity of the J-protein Sis1 in the propagation of 3 yeast prions. Proc Natl Acad Sci U S A 105(43):16596-601
Mandal AK, et al.  (2008) Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation. Mol Cell Biol 28(13):4434-44
Metzger MB, et al.  (2008) Degradation of a Cytosolic Protein Requires Endoplasmic Reticulum-associated Degradation Machinery. J Biol Chem 283(47):32302-16
Nakatsukasa K, et al.  (2008) Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 132(1):101-12
Needham PG and Masison DC  (2008) Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities. Arch Biochem Biophys 478(2):167-74
Shorter J and Lindquist S  (2008) Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions. EMBO J 27(20):2712-24
Tutar L and Tutar Y  (2008) Ydj1 but not Sis1 stabilizes Hsp70 protein under prolonged stress in vitro. Biopolymers 89(3):171-4
Weeks SA and Miller DJ  (2008) The heat shock protein 70 cochaperone YDJ1 is required for efficient membrane-specific flock house virus RNA replication complex assembly and function in Saccharomyces cerevisiae. J Virol 82(4):2004-12
Aldea M, et al.  (2007) Control of cell cycle and cell growth by molecular chaperones. Cell Cycle 6(21):2599-603
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
Verges E, et al.  (2007) Cyclin Cln3 Is Retained at the ER and Released by the J Chaperone Ydj1 in Late G1 to Trigger Cell Cycle Entry. Mol Cell 26(5):649-662
Ganem C, et al.  (2006) Kinase Cak1 functionally interacts with the PAF1 complex and phosphatase Ssu72 via kinases Ctk1 and Bur1. Mol Genet Genomics 275(2):136-47
Krzewska J and Melki R  (2006) Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J 25(4):822-33
Cashikar AG, et al.  (2005) A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem 280(25):23869-75
Fan CY, et al.  (2005) The type I Hsp40 zinc finger-like region is required for Hsp70 to capture non-native polypeptides from Ydj1. J Biol Chem 280(1):695-702
Haslbeck M, et al.  (2005) Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J Biol Chem 280(25):23861-8