메뉴 건너뛰기




Volumn 270, Issue 3, 1997, Pages 321-327

Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70

Author keywords

ATPase; GrpE; Hsp70; Mge1; Mitochondria; Molecular chaperones

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN 70;

EID: 0031577340     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1131     Document Type: Editorial
Times cited : (45)

References (31)
  • 1
    • 0029867559 scopus 로고    scopus 로고
    • Real time kinetics of the DnaK/DnaJ/GrpE molecular chaperone machine action
    • Banecki B., Zylicz M. Real time kinetics of the DnaK/DnaJ/GrpE molecular chaperone machine action. J. Biol. Chem. 271:1996;6137-6143.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6137-6143
    • Banecki, B.1    Zylicz, M.2
  • 4
    • 0029793330 scopus 로고    scopus 로고
    • Purification and biochemical properties ofSacchromyces cerevisiae's
    • Deloche O., Georgopoulos C. Purification and biochemical properties ofSacchromyces cerevisiae's. J. Biol. Chem. 271:1996;23960-23966.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23960-23966
    • Deloche, O.1    Georgopoulos, C.2
  • 5
    • 0027513927 scopus 로고
    • Nucleotide binding properties of bovine brain uncoating ATPase
    • Gao B., Emoto Y., Greene L., Eisenberg E. Nucleotide binding properties of bovine brain uncoating ATPase. J. Biol. Chem. 268:1993;8507-8513.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8507-8513
    • Gao, B.1    Emoto, Y.2    Greene, L.3    Eisenberg, E.4
  • 6
    • 0027333423 scopus 로고
    • Role of major heat shock proteins as molecular chaperones
    • Georgopoulos C., Welch W. J. Role of major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9:1993;601-634.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 7
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething M.-J., Sambrook J. Protein folding in the cell. Nature. 355:1992;33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 8
    • 0027184721 scopus 로고
    • Molecular chaperone function of heat-shock proteins
    • Hendrick J., Hartl F.-U. Molecular chaperone function of heat-shock proteins. Annu. Rev. Biochem. 62:1993;349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.1    Hartl, F.-U.2
  • 9
    • 0029875083 scopus 로고    scopus 로고
    • The mitochondrial protein import motor: Dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis
    • Horst M., Oppliger W., Feifel B., Schatz G., Glick B. S. The mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis. Protein Sci. 5:1996;759-767.
    • (1996) Protein Sci. , vol.5 , pp. 759-767
    • Horst, M.1    Oppliger, W.2    Feifel, B.3    Schatz, G.4    Glick, B.S.5
  • 11
    • 0028914392 scopus 로고
    • Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins
    • Jordan R., McMacken R. Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins. J. Biol. Chem. 270:1995;4563-4569.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4563-4569
    • Jordan, R.1    McMacken, R.2
  • 12
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang P. J., Ostermann J., Shilling J., Neupert W., Craig E. A., Pfanner N. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature. 348:1990;137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 13
    • 0028356858 scopus 로고
    • A role for a GrpE-related protein, Mge1, in protein translocation
    • Laloraya S., Gambill D. B., Craig E. A. A role for a GrpE-related protein, Mge1, in protein translocation. Proc. Natl Acad. Sci. USA. 91:1994;6481-6485.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 6481-6485
    • Laloraya, S.1    Gambill, D.B.2    Craig, E.A.3
  • 14
    • 0028850629 scopus 로고
    • Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of proteins
    • Laloraya S., Dekker P. J. T., Voos W., Craig E., Pfanner N. Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of proteins. Mol. Cell. Biol. 15:1995;7098-7105.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7098-7105
    • Laloraya, S.1    Dekker, P.J.T.2    Voos, W.3    Craig, E.4    Pfanner, N.5
  • 16
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty J. S., Buchberger A., Reinstein J., Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249:1995;126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 18
    • 0031556950 scopus 로고    scopus 로고
    • Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 ofSaccharomyces cerevisiae
    • Miao B., Davis J. E., Craig E. A. Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 ofSaccharomyces cerevisiae. J. Mol. Biol. 265:1997;541-552.
    • (1997) J. Mol. Biol. , vol.265 , pp. 541-552
    • Miao, B.1    Davis, J.E.2    Craig, E.A.3
  • 19
    • 0027172465 scopus 로고
    • Thermodynamic and structural analysis of the folding/unfolding transitions of theEscherichia coli
    • Montgomery D., Jordan R., McMacken R., Freire E. Thermodynamic and structural analysis of the folding/unfolding transitions of theEscherichia coli. J. Mol. Biol. 232:1993;680-692.
    • (1993) J. Mol. Biol. , vol.232 , pp. 680-692
    • Montgomery, D.1    Jordan, R.2    McMacken, R.3    Freire, E.4
  • 20
    • 0014307470 scopus 로고
    • Korrelation des unspezifisch permeablen mitochondrialen Raumes mit dem "Intermembran-Raum"
    • Pfaff E., Klingenberg M., Ritt E., Vogell W. Korrelation des unspezifisch permeablen mitochondrialen Raumes mit dem "Intermembran-Raum" Eur. J. Biochem. 5:1968;222-232.
    • (1968) Eur. J. Biochem. , vol.5 , pp. 222-232
    • Pfaff, E.1    Klingenberg, M.2    Ritt, E.3    Vogell, W.4
  • 21
    • 0030040712 scopus 로고    scopus 로고
    • Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation
    • Prip-Buus C., Westermann B., Schmitt M., Langer T., Neupert W., Schwarz E. Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation. FEBS Letters. 380:1996;142-146.
    • (1996) FEBS Letters. , vol.380 , pp. 142-146
    • Prip-Buus, C.1    Westermann, B.2    Schmitt, M.3    Langer, T.4    Neupert, W.5    Schwarz, E.6
  • 22
    • 0028046847 scopus 로고
    • Mitochondrial protein import: Biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44
    • Rassow J., Maarse A. C., Krainer E., Kübrich M., Müller H., Meijer M., Craig E. A., Pfanner N. Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44. J. Cell Biol. 127:1994;1547-1556.
    • (1994) J. Cell Biol. , vol.127 , pp. 1547-1556
    • Rassow, J.1    Maarse, A.C.2    Krainer, E.3    Kübrich, M.4    Müller, H.5    Meijer, M.6    Craig, E.A.7    Pfanner, N.8
  • 23
    • 0031106824 scopus 로고    scopus 로고
    • Molecular chaperones: Towards a characterization of the heat-shock protein 70 family
    • Rassow J., von Ahsen O., Bömer U., Pfanner N. Molecular chaperones: towards a characterization of the heat-shock protein 70 family. Trends Cell Biol. 7:1997;129-133.
    • (1997) Trends Cell Biol. , vol.7 , pp. 129-133
    • Rassow, J.1    Von Ahsen, O.2    Bömer, U.3    Pfanner, N.4
  • 24
    • 0028284879 scopus 로고
    • Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
    • Rowley N., Prip-Buus C., Westermann B., Brown C., Schwarz E., Barrell B., Neupert W. Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell. 77:1994;249-259.
    • (1994) Cell , vol.77 , pp. 249-259
    • Rowley, N.1    Prip-Buus, C.2    Westermann, B.3    Brown, C.4    Schwarz, E.5    Barrell, B.6    Neupert, W.7
  • 25
    • 0026799491 scopus 로고
    • Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange
    • Sadis S., Hightower L. Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange. Biochemistry. 31:1992;9406-9412.
    • (1992) Biochemistry , vol.31 , pp. 9406-9412
    • Sadis, S.1    Hightower, L.2
  • 26
    • 0025673942 scopus 로고
    • A precursor protein partly translocated into yeast mitochondria is bound to a 70 kD mitochondrial stress protein
    • Scherer P. E., Krieg U. C., Hwang S. T., Vestweber D., Schatz G. A precursor protein partly translocated into yeast mitochondria is bound to a 70 kD mitochondrial stress protein. EMBO J. 9:1990;4315-4322.
    • (1990) EMBO J. , vol.9 , pp. 4315-4322
    • Scherer, P.E.1    Krieg, U.C.2    Hwang, S.T.3    Vestweber, D.4    Schatz, G.5
  • 29
    • 0029583409 scopus 로고
    • The mitochondrial protein import machinery: Role of ATP in dissociation of the Hsp70-Mim44 complex
    • 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. 270:1995;29848-29853.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29848-29853
    • Von Ahsen, O.1    Voos, W.2    Henninger, H.3    Pfanner, N.4
  • 30
    • 0027994692 scopus 로고
    • Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes
    • Voos W., Gambill B. D., Laloraya S., Ang D., Craig E. A., Pfanner N. Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes. Mol. Cell. Biol. 14:1994;6627-6634.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6627-6634
    • Voos, W.1    Gambill, B.D.2    Laloraya, S.3    Ang, D.4    Craig, E.A.5    Pfanner, N.6
  • 31
    • 0001341839 scopus 로고
    • The role of the GrpE homologue, Mge1, in mediating protein import and protein folding in mitochondria
    • Westerman B., Prip-Buus C., Neupert W., Schwarz E. The role of the GrpE homologue, Mge1, in mediating protein import and protein folding in mitochondria. EMBO J. 13:1995;1998-2006.
    • (1995) EMBO J. , vol.13 , pp. 1998-2006
    • Westerman, B.1    Prip-Buus, C.2    Neupert, W.3    Schwarz, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.