Machinery for protein sorting and assembly in the mitochondrial outer membrane

Nature

Volumn 424, Issue 6948, 2003, Pages 565-571

  Wiedemann, Nils ^a   Kozjak, Vera ^a   Chacinska, Agnieszka ^a   Schönfisch, Birgit ^a   Rospert, Sabine ^b   Ryan, Michael T ^a,c   Pfanner, Nikolaus ^a   Meisinger, Chris ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

^c LA TROBE UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CELLS; ENZYMES;

MITOCHONDRIA;

PROTEINS;

CARRIER PROTEIN; MEMBRANE PROTEIN; PROTEIN PRECURSOR; SACCHAROMYCES CEREVISIAE PROTEIN; TOM37 PROTEIN, S CEREVISIAE; TOM40 PROTEIN, S CEREVISIAE;

MITOCHONDRIAL DNA; PROTEIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; MITOCHONDRIAL MEMBRANE; NONHUMAN; PLEIOTROPY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FUNCTION; BIOSYNTHESIS; CYTOLOGY; GENE DELETION; GENETICS; INTRACELLULAR MEMBRANE; MACROMOLECULE; METABOLISM; MITOCHONDRION; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE;

ANIMALIA;

GENE DELETION; INTRACELLULAR MEMBRANES; MACROMOLECULAR SUBSTANCES; MEMBRANE PROTEINS; MEMBRANE TRANSPORT PROTEINS; MITOCHONDRIA; PROTEIN PRECURSORS; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 0042163218     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01753     Document Type: Article

References (24)

1. Koehler, C. M., Merchant, S. & Schatz, G. How membrane proteins travel across the mitochondrial intermembrane space. Trends Biochem. Sci. 24, 428-432 (1999).
2. Herrmann, J. M. & Neupert, W. Protein transport into mitochondria. Curr. Opin. Microbiol. 3, 210-214 (2000).
3. Jensen, R. E. & Johnson, A. E. Opening the door to mitochondrial protein import. Nature Struct. Biol. 8, 1008-1010 (2001).
4. Endo, T. & Kohda, D. Functions of outer membrane receptors in mitochondrial protein import. Biochim. Biophys. Acta 1592, 3-14 (2002).
5. Pfanner, N. & Geissler, A. Versatility of the mitochondrial protein import machinery. Nature Rev. Mol. Cell. Biol. 2, 339-349 (2001).
6. Rapaport, D. & Neupert, W. Biogenesis of Tom40, core component of the TOM complex of mitochondria. J. Cell Biol. 146, 321-331 (1999).
7. Model, K. et al. Multistep assembly of the protein import channel of the mitochondrial outer membrane. Nature Struct. Biol. 8, 361-370 (2001).
8. Krimmer, T. et al. Biogenesis of porin of the outer mitochondrial membrane involves an import pathway via receptors and the general import pore of the TOM complex. J. Cell Biol. 152, 289-300 (2001).
9. Taylor, R. D., McHale, B. J. & Nargang, F. E. Characterization of neurospora crassa Tom40 deficient mutants and effect of specific mutations on Tom40 assembly. J. Biol. Chem. 278, 765-775 (2003).
10. Rapaport, D. Biogenesis of the mitochondrial TOM complex. Trends Biochem. Sci. 27, 191-197 (2002).
11. Gratzer, S. et al. Mas37p, a novel receptor subunit for protein import into mitochondria. J. Cell Biol. 129, 25-34 (1995).
12. Hachiya, N. et al. Reconstitution of the initial steps of mitochondrial protein import. Nature 376, 705-709 (1995).
13. Ryan, M. T., Müller, H. & Pfanner, N. Functional staging of ADP/ATP carrier translocation across the outer mitochondrial membrane. J. Biol Chem. 274, 20619-20627 (1999).
14. Abdul, K. M. et al. Functional analysis of human metaxin in mitochondrial protein import in cultured cells and its relationship with the Tom complex. Biochem. Biophys. Res. Commun. 276, 1028-1034 (2000).
15. Lithgow, T., Junne, T., Suda, K., Gratzer, S. & Schatz, G. The mitochondrial outer membrane protein Mas22p is essential for protein import and viability of yeast. Proc. Natl Acad. Sci. USA 91, 11973-11977 (1994).
16. Dekker, P. J. T. et al. The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44. EMBO J. 16, 5408-5419 (1997).
17. Dietmeier, K. et al. Tom5 functionally links mitochondrial preprotein receptors to the general import pore. Nature 388, 195-200 (1997).
18. Sogo, L. F. & Yaffe, M. P. Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J. Cell Biol. 126, 1361-1373 (1994).
19. Martelli, P. L., Fariselli, P., Krogh, A. & Casadio, R. A sequence-profile-based HMM for predicting and discriminating β barrel membrane proteins. Bioinformatics 18 (Suppl. 1), S46-S53 (2002).
20. Sesaki, H. & Jensen, R. E. UGO1 encodes an outer membrane protein required for mitochondrial fusion. J. Cell Biol. 152, 1123-1134 (2001).
21. van Wilpe, S. et al. Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase. Nature 401, 485-489 (1999).
22. Meisinger, C. et al. Protein import channel of the outer mitochondrial membrane: a highly stable Tom40-Tom22 core structure differentially interacts with preproteins, small Tom proteins, and import receptors. Mol. Cell. Biol. 21, 2337-2348 (2001).
23. Matouschek, A. & Glick, B. S. Barreling through the outer membrane. Nature Struct. Biol. 8, 284-286 (2001).
24. Hill, K. et al. Tom40 forms the hydrophilic channel of the mitochondrial import pore for preproteins. Nature 395, 516-521 (1998).