Genomes and Genes
Gene Symbol: MGE1
Alias: YGE1, Mge1p
Species: Saccharomyces cerevisiae S288c
- Blamowska M, Sichting M, Mapa K, Mokranjac D, Neupert W, Hell K. ATPase domain and interdomain linker play a key role in aggregation of mitochondrial Hsp70 chaperone Ssc1. J Biol Chem. 2010;285:4423-31 pubmed publisher..In conclusion, our results suggest that interdomain communication makes Ssc1 prone to aggregation. Hep1 counteracts aggregation by binding to this aggregation-prone conformer. ..
- Miao B, Davis J, Craig E. Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae. J Mol Biol. 1997;265:541-52 pubmedb>Mge1, a GrpE-related protein in the mitochondrial matrix of the budding yeast Saccharomyces cerevisiae, is required for translocation of precursor proteins into mitochondria...
- Laloraya S, Dekker P, Voos W, Craig E, Pfanner N. Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins. Mol Cell Biol. 1995;15:7098-105 pubmedMitochondrial GrpE (Mge1p) is a mitochondrial cochaperone essential for viability of the yeast Saccharomyces cerevisiae...
- Sakuragi S, Liu Q, Craig E. Interaction between the nucleotide exchange factor Mge1 and the mitochondrial Hsp70 Ssc1. J Biol Chem. 1999;274:11275-82 pubmed..and Ssc1 of the mitochondrial matrix of Saccharomyces cerevisiae requires the nucleotide release factors, GrpE and Mge1, respectively...
- Mokranjac D, Sichting M, Neupert W, Hell K. Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria. EMBO J. 2003;22:4945-56 pubmed..We propose a model in which Tim14 is required for the activation of mtHsp70 and enables this chaperone to act in a rapid and regulated manner in the Tim44-mediated trapping of unfolded preproteins entering the matrix. ..
- von Ahsen O, Voos W, Henninger H, Pfanner N. The mitochondrial protein import machinery. Role of ATP in dissociation of the Hsp70.Mim44 complex. J Biol Chem. 1995;270:29848-53 pubmed..We conclude that binding of ATP, not hydrolysis, is required to dissociate the mt-Hsp70.Mim44 complex and that the reaction cycle includes an ATP-induced conformational change of mt-Hsp70. ..
- Vögtle F, Wortelkamp S, Zahedi R, Becker D, Leidhold C, Gevaert K, et al. Global analysis of the mitochondrial N-proteome identifies a processing peptidase critical for protein stability. Cell. 2009;139:428-39 pubmed publisher..Our results suggest that Icp55 is critical for stabilization of the mitochondrial proteome and illustrate how the N-proteome can serve as rich source for a systematic analysis of mitochondrial protein targeting, cleavage and turnover. ..
- Sikor M, Mapa K, von Voithenberg L, Mokranjac D, Lamb D. Real-time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET. EMBO J. 2013;32:1639-49 pubmed publisher..The nucleotide-exchange factor Mge1 did not induce ADP release, as expected, but rather facilitated binding of ATP...
- Schneider H, Berthold J, Bauer M, Dietmeier K, Guiard B, Brunner M, et al. Mitochondrial Hsp70/MIM44 complex facilitates protein import. Nature. 1994;371:768-74 pubmed..The complex appears to act as a molecular ratchet which is energetically driven by the hydrolysis of ATP. ..
- Schmidt S, Strub A, Rottgers K, Zufall N, Voos W. The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1. J Mol Biol. 2001;313:13-26 pubmed..interaction with the preprotein translocase subunit Tim44, the cochaperone Mdj1, and the nucleotide exchange factor Mge1. In contrast, only limited information is available on Ssq1...
- Adam A, Bornhovd C, Prokisch H, Neupert W, Hell K. The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria. EMBO J. 2006;25:174-83 pubmed..In the absence of Isd11, Nfs1 is prone to aggregation. We propose that Isd11 acts together with Nfs1 in an early step in the biogenesis of Fe/S proteins. ..
- Baumann F, Milisav I, Neupert W, Herrmann J. Ecm10, a novel hsp70 homolog in the mitochondrial matrix of the yeast Saccharomyces cerevisiae. FEBS Lett. 2000;487:307-12 pubmed..Like Ssc1, Ecm10 interacts with the nucleotide exchange factor Mge1 in an ATP-dependent manner...
- Allu P, Marada A, Boggula Y, Karri S, Krishnamoorthy T, Sepuri N. Methionine sulfoxide reductase 2 reversibly regulates Mge1, a cochaperone of mitochondrial Hsp70, during oxidative stress. Mol Biol Cell. 2015;26:406-19 pubmed publisher..Our earlier studies showed that Mge1, an evolutionarily conserved nucleotide exchange factor of Hsp70, acts as an oxidative sensor to regulate ..
- Kubo Y, Tsunehiro T, Nishikawa S, Nakai M, Ikeda E, Toh e A, et al. Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system. J Mol Biol. 1999;286:447-64 pubmed..We have observed a similar two-pathway reactivation of heat-denatured luciferase by the bacterial Hsp70 and the yeast cytosolic Hsp70 systems. ..
- Merlin A, von Ahsen O, Craig E, Dietmeier K, Pfanner N. A mutant form of mitochondrial GrpE suppresses the sorting defect caused by an alteration in the presequence of cytochrome b2. J Mol Biol. 1997;273:1-6 pubmed..Together with its co-chaperone mitochondrial GrpE (Mge1), mtHsp70 transiently binds to the inner membrane translocase subunit Tim44 in a nucleotide-regulated manner, ..
- Horst M, Oppliger W, Rospert S, Schönfeld H, Schatz G, Azem A. Sequential action of two hsp70 complexes during protein import into mitochondria. EMBO J. 1997;16:1842-9 pubmed..A precursor protein entering the matrix interacts first with the import complex and then with the folding complex. A chaperone can thus function as part of two different complexes within the same organelle. ..
- Bolliger L, Deloche O, Glick B, Georgopoulos C, Jeno P, Kronidou N, et al. A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability. EMBO J. 1994;13:1998-2006 pubmed..Yeast GrpEp is made as a precursor that is cleaved upon import into isolated mitochondria. GrpEp is essential for viability. We suggest that this protein interacts with mhsp70 in a manner analogous to that of GrpE with DnaK of E.coli. ..
- Marada A, Karri S, Singh S, Allu P, Boggula Y, Krishnamoorthy T, et al. A Single Point Mutation in Mitochondrial Hsp70 Cochaperone Mge1 Gains Thermal Stability and Resistance. Biochemistry. 2016;55:7065-7072 pubmed publisherb>Mge1, a yeast homologue of Escherichia coli GrpE, is an evolutionarily conserved homodimeric nucleotide exchange factor of mitochondrial Hsp70...
- Geissler A, Rassow J, Pfanner N, Voos W. Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins. Mol Cell Biol. 2001;21:7097-104 pubmed
- Sichting M, Mokranjac D, Azem A, Neupert W, Hell K. Maintenance of structure and function of mitochondrial Hsp70 chaperones requires the chaperone Hep1. EMBO J. 2005;24:1046-56 pubmed..This process is efficiently counteracted by Hep1. We conclude that Hep1 acts as a chaperone that is necessary and sufficient to prevent self-aggregation and to thereby maintain the function of the mitochondrial Hsp70 chaperones. ..
- Marada A, Allu P, Murari A, Pullareddy B, Tammineni P, Thiriveedi V, et al. Mge1, a nucleotide exchange factor of Hsp70, acts as an oxidative sensor to regulate mitochondrial Hsp70 function. Mol Biol Cell. 2013;24:692-703 pubmed publisher..Dimeric yeast Mge1, the cochaperone of heat shock protein 70 (Hsp70), is essential for exchanging ATP for ADP on Hsp70 and thus for ..
- Voos W, Gambill B, Laloraya S, Ang D, Craig E, Pfanner N. Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes. Mol Cell Biol. 1994;14:6627-34 pubmed..After being imported into the matrix, the preprotein could be coprecipitated only by antibodies against mt-hsp70. We propose that mt-hsp70 and MGE cooperate in membrane translocation of preproteins. ..
- Chacinska A, Rehling P, Guiard B, Frazier A, Schulze Specking A, Pfanner N, et al. Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex. EMBO J. 2003;22:5370-81 pubmed..Thus, Tim50 functions as a dynamic factor and the IMS domain of Tom22 represents a stabilizing element in formation of a productive translocation contact site supercomplex. ..
- Nakai M, Kato Y, Ikeda E, Toh e A, Endo T. Yge1p, a eukaryotic Grp-E homolog, is localized in the mitochondrial matrix and interacts with mitochondrial Hsp70. Biochem Biophys Res Commun. 1994;200:435-42 pubmedYeast Yge1p, the gene product of YGE1, is a eukaryotic GrpE homolog found recently (Ikeda et al., 1994). We have revealed here that Yge1p is a soluble protein in the mitochondrial matrix...