MGE1/YOR232W Literature Guide Help

Other names published for MGE1: YGE1, GRPE, YOR232W

MGE1 - Function/Process (40)

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
Pareek G, et al.  (2011) Primary sequence that determines the functional overlap between mitochondrial heat shock protein 70 Ssc1 and Ssc3 of Saccharomyces cerevisiae. J Biol Chem 286(21):19001-13
Becker D, et al.  (2008) In vitro analysis of the mitochondrial preprotein import machinery using recombinant precursor polypeptides. Methods Mol Biol 457():59-83
Dutkiewicz R, et al.  (2006) The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p. J Biol Chem 281(12):7801-8
Altmann K and Westermann B  (2005) Role of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae. Mol Biol Cell 16(11):5410-7
Frazier AE, et al.  (2004) Pam16 has an essential role in the mitochondrial protein import motor. Nat Struct Mol Biol 11(3):226-33
Kozany C, et al.  (2004) The J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase. Nat Struct Mol Biol 11(3):234-41
Li Y, et al.  (2004) The presequence translocase-associated protein import motor of mitochondria. Pam16 functions in an antagonistic manner to Pam18. J Biol Chem 279(36):38047-54
Dutkiewicz R, et al.  (2003) Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart. J Biol Chem 278(32):29719-27
Liu Q, et al.  (2003) Regulated cycling of mitochondrial Hsp70 at the protein import channel. Science 300(5616):139-41
Truscott KN, et al.  (2003) A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria. J Cell Biol 163(4):707-13
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
Moro F, et al.  (2002) Mitochondrial protein import: molecular basis of the ATP-dependent interaction of MtHsp70 with Tim44. J Biol Chem 277(9):6874-80
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
Geissler A, et al.  (2001) Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins. Mol Cell Biol 21(20):7097-104
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
Geissler A, et al.  (2000) Biogenesis of the yeast frataxin homolog Yfh1p. Tim44-dependent transfer to mtHsp70 facilitates folding of newly imported proteins in mitochondria. Eur J Biochem 267(11):3167-80
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
Sakuragi S, et al.  (1999) Interaction between the nucleotide exchange factor Mge1 and the mitochondrial Hsp70 Ssc1. J Biol Chem 274(16):11275-82
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
Dekker PJ and Pfanner N  (1997) Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70. J Mol Biol 270(3):321-7
Horst M, et al.  (1997) Sequential action of two hsp70 complexes during protein import into mitochondria. EMBO J 16(8):1842-9
Merlin A, et al.  (1997) A mutant form of mitochondrial GrpE suppresses the sorting defect caused by an alteration in the presequence of cytochrome b2. J Mol Biol 273(1):1-6
Miao B, et al.  (1997) Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae. J Mol Biol 265(5):541-52
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