MDJ1/YFL016C Literature Guide Help

Other names published for MDJ1: YFL016C

MDJ1 - Function/Process (26)

ReferenceOther Genes Addressed
Iosefson O, et al.  (2012) Reactivation of protein aggregates by mortalin and Tid1--the human mitochondrial Hsp70 chaperone system. Cell Stress Chaperones 17(1):57-66
Schilke BA, et al.  (2012) Genetic analysis of complex interactions among components of the mitochondrial import motor and translocon in Saccharomyces cerevisiae. Genetics 190(4):1341-53
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
Lu B, et al.  (2006) Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate. J Biol Chem 281(19):13150-8
Dimmer KS, et al.  (2002) Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell 13(3):847-53
Germaniuk A, et al.  (2002) A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase. J Biol Chem 277(31):27801-8
Voos W and Rottgers K  (2002) Molecular chaperones as essential mediators of mitochondrial biogenesis. Biochim Biophys Acta 1592(1):51-62
Weiss C, et al.  (2002) Two-step purification of mitochondrial Hsp70, Ssc1p, using Mge1(His)(6) immobilized on Ni-agarose. Protein Expr Purif 24(2):268-73
Kawai A, et al.  (2001) Loss of the mitochondrial Hsp70 functions causes aggregation of mitochondria in yeast cells. J Cell Sci 114(Pt 19):3565-74
Krzewska J, et al.  (2001) Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein. J Mol Biol 314(4):901-10
Krzewska J, et al.  (2001) Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding. FEBS Lett 489(1):92-6
Liu Q, et al.  (2001) Mitochondrial Hsp70 Ssc1: role in protein folding. J Biol Chem 276(9):6112-8
Lutz T, et al.  (2001) The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria. J Mol Biol 307(3):815-25
Schmidt S, et al.  (2001) The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1. J Mol Biol 313(1):13-26
Lisse T and Schwarz E  (2000) Functional specificity of the mitochondrial DnaJ protein, Mdj1p, in Saccharomyces cerevisiae. Mol Gen Genet 263(3):527-34
Duchniewicz M, et al.  (1999) Dual role of the mitochondrial chaperone Mdj1p in inheritance of mitochondrial DNA in yeast. Mol Cell Biol 19(12):8201-10
Kubo Y, et al.  (1999) Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol 286(2):447-64
Savel'ev AS, et al.  (1998) ATP-dependent proteolysis in mitochondria. m-AAA protease and PIM1 protease exert overlapping substrate specificities and cooperate with the mtHsp70 system. J Biol Chem 273(32):20596-602
Deloche O, et al.  (1997) Purification and biochemical properties of Saccharomyces cerevisiae Mdj1p, the mitochondrial DnaJ homologue. J Biol Chem 272(45):28539-44
Horst M, et al.  (1997) Sequential action of two hsp70 complexes during protein import into mitochondria. EMBO J 16(8):1842-9
Westermann B and Neupert W  (1997) Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae. J Mol Biol 272(4):477-83
Deloche O and Georgopoulos C  (1996) Purification and biochemical properties of Saccharomyces cerevisiae's Mge1p, the mitochondrial cochaperone of Ssc1p. J Biol Chem 271(39):23960-6
Prip-Buus C, et al.  (1996) Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation. FEBS Lett 380(1-2):142-6
Westermann B, et al.  (1996) Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins. Mol Cell Biol 16(12):7063-71
Rowley N, et al.  (1994) Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77(2):249-59
Wagner I, et al.  (1994) Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21):5135-45