Mitochondrial import driving forces: Enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins

Molecular and Cellular Biology

Volumn 21, Issue 20, 2001, Pages 7097-7104

  Geissler, A ^a   Rassow, J ^a   Pfanner, N ^a   Voos, W ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 70; MUTANT PROTEIN; PROTEIN PRECURSOR;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; MEMBRANE POTENTIAL; MITOCHONDRIAL MEMBRANE; MITOCHONDRION; MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN TRANSPORT;

CALCIUM-TRANSPORTING ATPASES; CARRIER PROTEINS; CELL MEMBRANE; CISPLATIN; CROSS-LINKING REAGENTS; DOSE-RESPONSE RELATIONSHIP, DRUG; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FUNGAL PROTEINS; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MEMBRANE POTENTIALS; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; MITOCHONDRIA; MITOCHONDRIAL MEMBRANE TRANSPORT PROTEINS; MOLECULAR CHAPERONES; MUTATION; PRECIPITIN TESTS; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TIME FACTORS;

EID: 0034802764     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.21.20.7097-7104.2001     Document Type: Article

References (49)

1. Mitochondrial receptor complex from Neurospora crassa and Saccharomyces cerevisiae
2. Protein translocation into mitochondria: The role of TIM complexes
3. Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria
4. 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
5. The Hsp70 and Hsp60 chaperone machines
6. A matrix ATP requirement for presequence translocation across the inner membrane of mitochondria
7. Molecular chaperones
8. A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins
9. Mitochondrial import of subunit Va of cytochrome c oxidase characterized with yeast mutants. Independence from receptors, but requirement for matrix hsp70 translocase function
10. Unfolding of preproteins upon import into mitochondria
11. 2 modulates the Δψ-dependence of translocation of the matrix-targeting sequence
12. Biogenesis of the yeast frataxin homolog Yfh1p: Tim44-dependent transfer to mtHsp70 facilitates folding of newly imported proteins in mitochondria
13. Can Hsp70 proteins act as force-generating motors?
14. 2 to the mitochondrial intermembrane space: The tightly folded heme-binding domain makes import dependent upon matrix ATP
15. Molecular chaperones in cellular protein folding
16. Reconstitution of the protein insertion machinery of the mitochondrial inner membrane
17. The mitochondrial protein import motor: Dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysis
18. Mitochondria unfold precursor proteins by unraveling them from their N-termini
19. Protein translocation: Is Hsp70 pulling my chain?
20. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
21. Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane
22. The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation
23. Mitochondrial Hsp70 Ssc1: Role in protein folding
24. Role of an energized inner membrane in mitochondrial protein import: Δψ drives the movement of presequences
25. BiP acts as a molecular ratchet during posttranslational transport of prepro-α factor across the ER membrane
26. Active unfolding of precursor proteins during mitochondrial protein import
27. The TIM17-23 preprotein translocase of mitochondria: Composition and function in protein transport into the matrix
28. Protein import into mitochondria
29. Folding of active β-lactamase in the yeast cytoplasm before translocation into the endoplasmic reticulum
30. Mitochondrial preprotein translocase
31. Protein sorting: Pulling in the proteins
32. Transport of proteins into mitochondria: A potassium diffusion potential is able to drive the import of ADP/ATP carrier
33. Protein translocation: How Hsp70 pulls it off
34. Mitochondrial protein import: Biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein M1M44
35. Common principles of protein translocation across membranes
36. A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein
37. Transport of proteins into mitochondria: Translocational intermediates spanning contact sites between outer and inner membranes
38. Mitochondrial Hsp70/MIM44 complex facilitates protein import
39. The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import
40. Analysis of mitochondrial protein import using translocation intermediates and specific: Antibodies
41. The Δψ- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria
42. The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria
43. Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast
44. The protein import motor of mitochondria: Unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70
45. The mitochondrial protein import machinery: Role of ATP in dissociation of the Hsp70-Mim44 complex
46. Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes
47. Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix
48. Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins
49. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane