Molecular chaperones as essential mediators of mitochondrial biogenesis

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1592, Issue 1, 2002, Pages 51-62

  Voos, Wolfgang ^a   Röttgers, Karin ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

Clp Hsp100; Degradation; Hsp60; Hsp70; Membrane translocation; Mitochondrion

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; PROTEIN; PROTEIN MDJ1; PROTEIN MGE1; PROTEIN SSQ1; PROTEIN TIM44; UNCLASSIFIED DRUG;

BIOGENESIS; HYDROLYSIS; MITOCHONDRIAL MEMBRANE; MITOCHONDRION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; REVIEW; STRESS;

CALCIUM-TRANSPORTING ATPASES; CYTOSOL; HSP70 HEAT-SHOCK PROTEINS; INTRACELLULAR MEMBRANES; MEMBRANE POTENTIALS; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; MOLECULAR CHAPERONES; PROTEIN FOLDING; PROTEIN PRECURSORS; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 0037009130     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(02)00264-1     Document Type: Review

References (112)

1. The Hsp70 and Hsp60 chaperone machines
2. Protein folding in the cytosol: Chaperonin-dependent and -independent mechanisms
3. Molecular chaperones in cellular protein folding
4. Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones
5. HSP100/Clp proteins: A common mechanism explains diverse functions
6. Molecular chaperones: Towards a characterization of the heat-shock protein 70 family
7. SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth
8. The mitochondrial protein import machinery. Role of ATP in dissociation of the Hsp70.Mim44 complex
9. Molecular basis for interactions of the DnaK chaperone with substrates
10. Polypeptides traverse the mitochondrial envelope in an extended state
11. The structure of precursor proteins during import into mitochondria
12. The dimensions of the protein import channels in the outer and inner mitochondrial membranes
13. Genetic and biochemical dissection of the mitochondrial protein-import machinery
14. A precursor protein partly translocated into yeast mitochondria is bound to a 70 kD mitochondrial stress protein
15. A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins
16. Membrane potential-driven protein import into mitochondria. The sorting sequence of cytochrome b(2) modulates the deltapsi-dependence of translocation of the matrix-targeting sequence
17. Role of an energized inner membrane in mitochondrial protein import
18. Protein import into mitochondria: The requirement for external ATP is precursor-specific whereas intramitochondrial ATP is universally needed for translocation into the matrix
19. A matrix ATP requirement for presequence translocation across the inner membrane of mitochondria
20. Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix
21. The requirement of matrix ATP for the import of precursor proteins into the mitochondrial matrix and intermembrane space
22. Multiple interactions of components mediating preprotein translocation across the inner mitochondrial membrane
23. A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability
24. Yge1p, a eukaryotic GrpE-homolog, is localized in the mitochondrial matrix and interacts with mitochondrial hsp70
25. Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae
26. Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70
27. Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins
28. A role for a eukaryotic GrpE-related protein Mge1p, in protein translocation
29. The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria
30. Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes
31. The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import
32. MPI1, an essential gene encoding a mitochondrial membrane protein, is possibly involved in protein import into yeast mitochondria
33. Identification of a 45-kDa protein import site of the yeast mitochondrial inner membrane
34. The essential yeast protein MIM44 (encoded by MPI1) is involved in an early step of preprotein translocation across the mitochondrial inner membrane
35. Domain structure and lipid interaction of recombinant yeast Tim44
36. Mitochondrial protein import: Biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44
37. Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane
38. Mitochondrial Hsp70/MIM44 complex facilitates protein import
39. Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae
40. The J-related segment of Tim44 is essential for cell viability: A mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation
41. The mitochondrial protein import motor: Dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis
42. Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins
43. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
44. Mitochondrial protein import motor: The ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role
45. The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria
46. The delta psi- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria
47. Separation of structural and dynamic functions of the mitochondrial translocase: Tim44 is crucial for the inner membrane import sites in translocation of tightly folded domains, but not of loosely folded preproteins
48. What drives the translocation of proteins?
49. The role of hsp70 in conferring unidirectionality on protein translocation
50. Modular structure of the TIM23 preprotein translocase of mitochondria
51. Protein translocation into mitochondria: The role of TIM complexes
52. Mitochondrial import driving forces: Enhanced trapping by matrix hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins
53. Can Hsp70 proteins act as force-generating motors?
54. Protein sorting: Pulling in the proteins
55. A conserved domain in Escherichia coli Lon protease is involved in substrate discriminator activity
56. Recognition of preproteins by the isolated TOM complex of mitochondria
57. Effect of the protein import machinery at the mitochondrial surface on precursor stability
58. 2 to the mitochondrial intermembrane space: The tightly folded heme-binding domain makes import dependent upon matrix ATP
59. Unfolding of preproteins upon import into mitochondria
60. Mitochondria unfold precursor proteins by unraveling them from their N-termini
61. The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation
62. Active unfolding of precursor proteins during mitochondrial protein import
63. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
64. The protein import motor of mitochondria: Unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70
65. Protein unfolding by mitochondria. The Hsp70 import motor
66. Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA
67. Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
68. Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast Saccharomyces cerevisiae
69. Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation
70. Sequential action of two hsp70 complexes during protein import into mitochondria
71. Two distinct mechanisms operate in the reactivation of heat-denatured proteins by the mitochondrial Hsp70/Mdj1p/Yge1p chaperone system
72. Dual role of the mitochondrial chaperone Mdj1p in inheritance of mitochondrial DNA in yeast
73. Ecm10, a novel Hsp70 homolog in the mitochondrial matrix of the yeast Saccharomyces cerevisiae
74. The cold sensitivity of a mutant of Saccharomyces cerevisiae lacking a mitochondrial heat shock protein 70 is suppressed by loss of mitochondrial DNA
75. Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
76. The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria
77. Biogenesis of iron-sulfur proteins in eukaryotes: A novel task of mitochondria that is inherited from bacteria
78. Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
79. Role of the mitochondrial Hsp70s, Ssc1 and Ssq1, in the maturation of Yfh1
80. The two mitochondrial heat shock proteins 70, Ssc1 and Ssq1, compete for the cochaperone Mge1
81. Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly
82. Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae
83. J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins
84. Molecular chaperones and mitochondrial protein folding
85. Structure and function in GroEL-mediated protein folding
86. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
87. Identification of a groES-like chaperonin in mitochondria that facilitates protein folding
88. Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES
89. Putting a lid on protein folding: Structure and function of the co-chaperonin, GroES
90. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
91. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
92. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
93. Directionality of polypeptide transfer in the mitochondrial pathway of chaperone-mediated protein folding
94. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10
95. Hsp60-independent protein folding in the matrix of yeast mitochondria
96. Sequential action of mitochondrial chaperones in protein import into mitochondria
97. Cyclophilin catalyzes protein folding in yeast mitochondria
98. Cyclophilin 20, is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60
99. The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form
100. Molecular chaperones. Resurrection or destruction?
101. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
102. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli
103. Heat-shock protein 104 expression is sufficient for thermotolerance in yeast
104. Protein disaggregation mediated by heat-shock protein Hsp104
105. HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases
106. Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70
107. The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function
108. The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria
109. Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding
110. Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae
111. A human homologue of Escherichia coli ClpP caseinolytic protease: Recombinant expression, intracellular processing and subcellular localization
112. AAA proteases: Cellular machines for degrading membrane proteins