publication . Article . 2011

Reevaluation of the role of the Pam18:Pam16 interaction in translocation of proteins by the mitochondrial Hsp70-based import motor

June E. Pais; Brenda Schilke; Elizabeth A. Craig;
Open Access English
  • Published: 15 Dec 2011 Journal: Molecular Biology of the Cell, volume 22, issue 24, pages 4,740-4,749 (issn: 1059-1524, eissn: 1939-4586, Copyright policy)
  • Publisher: The American Society for Cell Biology
Abstract
The heat-shock protein 70 (Hsp70)–based import motor, associated with the translocon on the matrix side of the mitochondrial inner membrane, drives translocation of proteins via cycles of binding and release. Stimulation of Hsp70's ATPase activity by the translocon-associated J-protein Pam18 is critical for this process. Pam18 forms a heterodimer with the structurally related protein Pam16, via their J-type domains. This interaction has been proposed to perform a critical regulatory function, inhibiting the ATPase stimulatory activity of Pam18. Using biochemical and genetic assays, we tested this hypothesis by assessing the in vivo function of Pam18 variants hav...
Subjects
Medical Subject Headings: lipids (amino acids, peptides, and proteins)
free text keywords: Articles, Biosynthesis and Biodegradation, Cell Biology, Molecular Biology, Saccharomyces cerevisiae, biology.organism_classification, biology, Membrane transport protein, biology.protein, ATPase, Translocon, Inner mitochondrial membrane, Mutation, medicine.disease_cause, medicine, Mitochondrial membrane transport protein, Transport protein
Funded by
NIH| CHARACTERIZATION OF TRANSCRIPTIONALLY REGULATED GENES
Project
  • Funder: National Institutes of Health (NIH)
  • Project Code: 5R01GM027870-12
  • Funding stream: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
,
NIH| Mechanism and regulation of the Hsp70-based mitochondrial protein import motor
Project
  • Funder: National Institutes of Health (NIH)
  • Project Code: 1F32GM087006-01
  • Funding stream: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
37 references, page 1 of 3

Bukau, B, Weissman, J, Horwich, A. Molecular chaperones and protein quality control. Cell. 2006; 125: 443-451 [PubMed]

Chacinska, A. Mitochondrial presequence translocase: switching between tom tethering and motor recruitment involves Tim21 and Tim17. Cell. 2005; 120: 817-829 [OpenAIRE] [PubMed]

Craig, EA, Huang, P, Aron, R, Andrew, A. The diverse roles of J-proteins, the obligate Hsp70 co-chaperone. Rev Physiol Biochem Pharmacol. 2006; 156: 1-21 [PubMed]

D'silva, P, Marszalek, J, Craig, EA. An essential connection: link between Hsp70's domains at last. Mol Cell. 2005a; 20: 493-494 [OpenAIRE] [PubMed]

D'silva, PD, Schilke, B, Walter, W, Andrew, A, Craig, EA. J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix. Proc Natl Acad Sci USA. 2003; 100: 13839-13844 [OpenAIRE] [PubMed]

D'silva, PR, Schilke, B, Hayashi, M, Craig, EA. Interaction of the J-protein heterodimer Pam18/Pam16 of the mitochondrial import motor with the translocon of the inner membrane. Mol Biol Cell. 2008; 19: 424-432 [OpenAIRE] [PubMed]

D'silva, PR, Schilke, B, Walter, W, Craig, EA. Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane. Proc Natl Acad Sci USA. 2005b; 102: 12419-12424 [OpenAIRE] [PubMed]

Endo, T, Yamano, K, Kawano, S. Structural insight into the mitochondrial protein import system. Biochim Biophys Acta. 2011; 1808: 955-970 [PubMed]

Frazier, AE. Pam16 has an essential role in the mitochondrial protein import motor. Nat Struct Mol Biol. 2004; 11: 226-233 [OpenAIRE] [PubMed]

Hutu, DP, Guiard, B, Chacinska, A, Becker, D, Pfanner, N, Rehling, P, van der Laan, M. Mitochondrial protein import motor: differential role of tim44 in the recruitment of Pam17 and J-complex to the presequence translocase. Mol Biol Cell. 2008; 19: 2642-2649 [OpenAIRE] [PubMed]

James, P, Pfund, C, Craig, EA. Functional specificity among Hsp70 molecular chaperones. Science. 1997; 275: 387-389 [PubMed]

Jensen, RE, Johnson, AE. Opening the door to mitochondrial protein import. Nat Struct Biol. 2001; 8: 1008-1010 [PubMed]

Koehler, CM. New developments in mitochondrial assembly. Annu Rev Cell Dev Biol. 2004; 20: 309-335 [PubMed]

Kozany, C, Mokranjac, D, Sichting, M, Neupert, W, Hell, K. The J domain-related cochaperone Tim16 is a constituent of the mitochondrial Tim23 preprotein translocase. Nat Struct Mol Biol. 2004; 11: 234-241 [OpenAIRE] [PubMed]

Laufen, T, Mayer, MP, Beisel, C, Klostermeier, D, Mogk, A, Reinstein, J, Bukau, B. Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones. Proc Natl Acad Sci USA. 1999; 96: 5452-5457 [OpenAIRE] [PubMed]

37 references, page 1 of 3
Abstract
The heat-shock protein 70 (Hsp70)–based import motor, associated with the translocon on the matrix side of the mitochondrial inner membrane, drives translocation of proteins via cycles of binding and release. Stimulation of Hsp70's ATPase activity by the translocon-associated J-protein Pam18 is critical for this process. Pam18 forms a heterodimer with the structurally related protein Pam16, via their J-type domains. This interaction has been proposed to perform a critical regulatory function, inhibiting the ATPase stimulatory activity of Pam18. Using biochemical and genetic assays, we tested this hypothesis by assessing the in vivo function of Pam18 variants hav...
Subjects
Medical Subject Headings: lipids (amino acids, peptides, and proteins)
free text keywords: Articles, Biosynthesis and Biodegradation, Cell Biology, Molecular Biology, Saccharomyces cerevisiae, biology.organism_classification, biology, Membrane transport protein, biology.protein, ATPase, Translocon, Inner mitochondrial membrane, Mutation, medicine.disease_cause, medicine, Mitochondrial membrane transport protein, Transport protein
Funded by
NIH| CHARACTERIZATION OF TRANSCRIPTIONALLY REGULATED GENES
Project
  • Funder: National Institutes of Health (NIH)
  • Project Code: 5R01GM027870-12
  • Funding stream: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
,
NIH| Mechanism and regulation of the Hsp70-based mitochondrial protein import motor
Project
  • Funder: National Institutes of Health (NIH)
  • Project Code: 1F32GM087006-01
  • Funding stream: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
37 references, page 1 of 3

Bukau, B, Weissman, J, Horwich, A. Molecular chaperones and protein quality control. Cell. 2006; 125: 443-451 [PubMed]

Chacinska, A. Mitochondrial presequence translocase: switching between tom tethering and motor recruitment involves Tim21 and Tim17. Cell. 2005; 120: 817-829 [OpenAIRE] [PubMed]

Craig, EA, Huang, P, Aron, R, Andrew, A. The diverse roles of J-proteins, the obligate Hsp70 co-chaperone. Rev Physiol Biochem Pharmacol. 2006; 156: 1-21 [PubMed]

D'silva, P, Marszalek, J, Craig, EA. An essential connection: link between Hsp70's domains at last. Mol Cell. 2005a; 20: 493-494 [OpenAIRE] [PubMed]

D'silva, PD, Schilke, B, Walter, W, Andrew, A, Craig, EA. J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix. Proc Natl Acad Sci USA. 2003; 100: 13839-13844 [OpenAIRE] [PubMed]

D'silva, PR, Schilke, B, Hayashi, M, Craig, EA. Interaction of the J-protein heterodimer Pam18/Pam16 of the mitochondrial import motor with the translocon of the inner membrane. Mol Biol Cell. 2008; 19: 424-432 [OpenAIRE] [PubMed]

D'silva, PR, Schilke, B, Walter, W, Craig, EA. Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane. Proc Natl Acad Sci USA. 2005b; 102: 12419-12424 [OpenAIRE] [PubMed]

Endo, T, Yamano, K, Kawano, S. Structural insight into the mitochondrial protein import system. Biochim Biophys Acta. 2011; 1808: 955-970 [PubMed]

Frazier, AE. Pam16 has an essential role in the mitochondrial protein import motor. Nat Struct Mol Biol. 2004; 11: 226-233 [OpenAIRE] [PubMed]

Hutu, DP, Guiard, B, Chacinska, A, Becker, D, Pfanner, N, Rehling, P, van der Laan, M. Mitochondrial protein import motor: differential role of tim44 in the recruitment of Pam17 and J-complex to the presequence translocase. Mol Biol Cell. 2008; 19: 2642-2649 [OpenAIRE] [PubMed]

James, P, Pfund, C, Craig, EA. Functional specificity among Hsp70 molecular chaperones. Science. 1997; 275: 387-389 [PubMed]

Jensen, RE, Johnson, AE. Opening the door to mitochondrial protein import. Nat Struct Biol. 2001; 8: 1008-1010 [PubMed]

Koehler, CM. New developments in mitochondrial assembly. Annu Rev Cell Dev Biol. 2004; 20: 309-335 [PubMed]

Kozany, C, Mokranjac, D, Sichting, M, Neupert, W, Hell, K. The J domain-related cochaperone Tim16 is a constituent of the mitochondrial Tim23 preprotein translocase. Nat Struct Mol Biol. 2004; 11: 234-241 [OpenAIRE] [PubMed]

Laufen, T, Mayer, MP, Beisel, C, Klostermeier, D, Mogk, A, Reinstein, J, Bukau, B. Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones. Proc Natl Acad Sci USA. 1999; 96: 5452-5457 [OpenAIRE] [PubMed]

37 references, page 1 of 3
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