Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Science Policy Alerts

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 13 December 1991:
Vol. 254. no. 5038, pp. 1659 - 1662
DOI: 10.1126/science.1661031
Prev | Table of Contents | Next

Articles

Science, Vol 254, Issue 5038, 1659-1662
Copyright © 1991 by American Association for the Advancement of Science

articles

Targeting of the master receptor MOM19 to mitochondria

H Schneider, T Sollner, K Dietmeier, C Eckerskorn, F Lottspeich, B Trulzsch, W Neupert, and N Pfanner

Institut fur Physiologische Chemie, Universitat Munchen, Germany.

The targeting of proteins to mitochondria involves the recognition of the precursor proteins by receptors on the mitochondrial surface followed by insertion of the precursors into the outer membrane at the general insertion site GIP. Most mitochondrial proteins analyzed so far use a mitochondrial outer membrane protein of 19 kilodaltons (MOM19) as an import receptor. The gene encoding MOM19 has now been isolated. The deduced amino acid sequence predicts that MOM19 is anchored in the outer membrane by an NH2-terminal hydrophobic sequence, while the rest of the protein forms a hydrophilic domain exposed to the cytosol. MOM19 was targeted to the mitochondria via a pathway that is independent of protease-accessible surface receptors and controlled by direct assembly of the MOM19 precursor with GIP.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Degradation of a Cytosolic Protein Requires Endoplasmic Reticulum-associated Degradation Machinery.
M. B. Metzger, M. J. Maurer, B. M. Dancy, and S. Michaelis (2008)
J. Biol. Chem. 283, 32302-32316
   Abstract »    Full Text »    PDF »
Biogenesis of the Mitochondrial TOM Complex: Mim1 PROMOTES INSERTION AND ASSEMBLY OF SIGNAL-ANCHORED RECEPTORS.
T. Becker, S. Pfannschmidt, B. Guiard, D. Stojanovski, D. Milenkovic, S. Kutik, N. Pfanner, C. Meisinger, and N. Wiedemann (2008)
J. Biol. Chem. 283, 120-127
   Abstract »    Full Text »    PDF »
Alternative function for the mitochondrial SAM complex in biogenesis of {alpha}-helical TOM proteins.
D. Stojanovski, B. Guiard, V. Kozjak-Pavlovic, N. Pfanner, and C. Meisinger (2007)
J. Cell Biol. 179, 881-893
   Abstract »    Full Text »    PDF »
How does the TOM complex mediate insertion of precursor proteins into the mitochondrial outer membrane?.
D. Rapaport (2005)
J. Cell Biol. 171, 419-423
   Abstract »    Full Text »    PDF »
Import of rat mitochondrial citrate carrier (CIC) at increasing salt concentrations promotes presequence binding to import receptor Tom20 and inhibits membrane translocation.
V. Zara, A. Ferramosca, P. Papatheodorou, F. Palmieri, and J. Rassow (2005)
J. Cell Sci. 118, 3985-3995
   Abstract »    Full Text »    PDF »
Signal-anchored Proteins Follow a Unique Insertion Pathway into the Outer Membrane of Mitochondria.
U. Ahting, T. Waizenegger, W. Neupert, and D. Rapaport (2005)
J. Biol. Chem. 280, 48-53
   Abstract »    Full Text »    PDF »
Import Pathways of Chloroplast Interior Proteins and the Outer-Membrane Protein OEP14 Converge at Toc75.
S.-L. Tu, L.-J. Chen, M. D. Smith, Y.-s. Su, D. J. Schnell, and H.-m. Li (2004)
PLANT CELL 16, 2078-2088
   Abstract »    Full Text »    PDF »
Targeting and Assembly of Rat Mitochondrial Translocase of Outer Membrane 22 (TOM22) into the TOM Complex.
Y. Nakamura, H. Suzuki, M. Sakaguchi, and K. Mihara (2004)
J. Biol. Chem. 279, 21223-21232
   Abstract »    Full Text »    PDF »
Biogenesis of the Protein Import Channel Tom40 of the Mitochondrial Outer Membrane: INTERMEMBRANE SPACE COMPONENTS ARE INVOLVED IN AN EARLY STAGE OF THE ASSEMBLY PATHWAY.
N. Wiedemann, K. N. Truscott, S. Pfannschmidt, B. Guiard, C. Meisinger, and N. Pfanner (2004)
J. Biol. Chem. 279, 18188-18194
   Abstract »    Full Text »    PDF »
Signal-Anchor Domains of Proteins of the Outer Membrane of Mitochondria: STRUCTURAL AND FUNCTIONAL CHARACTERISTICS.
T. Waizenegger, T. Stan, W. Neupert, and D. Rapaport (2003)
J. Biol. Chem. 278, 42064-42071
   Abstract »    Full Text »    PDF »
Targeting and Assembly of Mitochondrial Tail-anchored Protein Tom5 to the TOM Complex Depend on a Signal Distinct from That of Tail-anchored Proteins Dispersed in the Membrane.
C. Horie, H. Suzuki, M. Sakaguchi, and K. Mihara (2003)
J. Biol. Chem. 278, 41462-41471
   Abstract »    Full Text »    PDF »
Characterization of the signal that directs Bcl-xL, but not Bcl-2, to the mitochondrial outer membrane.
T. Kaufmann, S. Schlipf, J. Sanz, K. Neubert, R. Stein, and C. Borner (2003)
J. Cell Biol. 160, 53-64
   Abstract »    Full Text »    PDF »
Dual localization of human DNA topoisomerase IIIalpha to mitochondria and nucleus.
Y. Wang, Y. L. Lyu, and J. C. Wang (2002)
PNAS 99, 12114-12119
   Abstract »    Full Text »    PDF »
Characterization of Signal That Directs C-Tail-anchored Proteins to Mammalian Mitochondrial Outer Membrane.
C. Horie, H. Suzuki, M. Sakaguchi, and K. Mihara (2002)
Mol. Biol. Cell 13, 1615-1625
   Abstract »    Full Text »    PDF »
Characterization of the Signal that Directs Tom20 to the Mitochondrial Outer Membrane.
S. Kanaji, J. Iwahashi, Y. Kida, M. Sakaguchi, and K. Mihara (2000)
J. Cell Biol. 151, 277-288
   Abstract »    Full Text »    PDF »
Distribution of Binding Sequences for the Mitochondrial Import Receptors Tom20, Tom22, and Tom70 in a Presequence-carrying Preprotein and a Non-cleavable Preprotein.
J. Brix, S. Rudiger, B. Bukau, J. Schneider-Mergener, and N. Pfanner (1999)
J. Biol. Chem. 274, 16522-16530
   Abstract »    Full Text »    PDF »
Differential Recognition of Preproteins by the Purified Cytosolic Domains of the Mitochondrial Import Receptors Tom20, Tom22, and Tom70.
J. Brix, K. Dietmeier, and N. Pfanner (1997)
J. Biol. Chem. 272, 20730-20735
   Abstract »    Full Text »    PDF »
Interactions of the Human Mitochondrial Protein Import Receptor, hTom20, with Precursor Proteins in Vitro Reveal Pleiotropic Specificities and Different Receptor Domain Requirements.
E. Schleiff, G. C. Shore, and I. S. Goping (1997)
J. Biol. Chem. 272, 17784-17789
   Abstract »    Full Text »    PDF »
Signal Anchor Sequence Insertion into the Outer Mitochondrial Membrane. COMPARISON WITH PORIN AND THE MATRIX PROTEIN TARGETING PATHWAY.
D. G. Millar and G. C. Shore (1996)
J. Biol. Chem. 271, 25823-25829
   Abstract »    Full Text »    PDF »
Assembly of the Preprotein Receptor MOM72/MAS70 into the Protein Import Complex of the Outer Membrane of Mitochondria.
J. Schlossmann and W. Neupert (1995)
J. Biol. Chem. 270, 27116-27121
   Abstract »    Full Text »    PDF »
Biogenesis of ISP6, a Small Carboxyl-terminal Anchored Protein of the Receptor Complex of the Mitochondrial Outer Membrane.
W. Cao and M. G. Douglas (1995)
J. Biol. Chem. 270, 5674-5679
   Abstract »    Full Text »    PDF »
Mitochondrial Import of Subunit Va of Cytochrome c Oxidase Characterized with Yeast Mutants.
F. Gärtner, W. Voos, A. Querol, B. R. Miller, E. A. Craig, M. G. Cumsky, and N. Pfanner (1995)
J. Biol. Chem. 270, 3788-3795
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)