JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M307047200 on August 1, 2003

J. Biol. Chem., Vol. 278, Issue 42, 41462-41471, October 17, 2003
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
278/42/41462    most recent
M307047200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Horie, C.
Right arrow Articles by Mihara, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Horie, C.
Right arrow Articles by Mihara, K.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

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*

Chika Horie, Hiroyuki Suzuki, Masao Sakaguchi and Katsuyoshi Mihara {ddagger}

From the Department of Molecular Biology, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan

Mitochondrial outer membrane proteins are synthesized without a cleavable presequence but instead contain segments responsible for mitochondrial targeting and membrane integration within the molecule: the transmembrane segment (TMS) and N- or C-terminal flanking segment. We analyzed targeting and integration of Tom5, a C-tail anchor protein associated with the preprotein translocase of the outer membrane, to the yeast mitochondrial outer membrane in vivo using green fluorescent protein as the reporter and compared the signal with other signals for proteins dispersed in the membrane. The functional assembly of Tom5 into the TOM complex was assessed by blue native PAGE and complementation of temperature-sensitive {Delta}tom5 cells. Correct targeting and assembly required (i) an appropriate length TMS rather than hydrophobicity, (ii) a proline residue located at correct position in the TMS and specific residues near the proline, and (iii) that, in contrast to proteins dispersed in the outer membrane, the positive C-terminal segment was dispensable. Based on these findings, we constructed green fluorescent protein fusions with a C-terminal TMS in which the deduced sequences (minimum: Ser-Pro-Met) were inserted at an appropriate position within artificial Leu-Ala repeats. They were targeted to mitochondria and complemented the temperature-sensitive growth phenotype of {Delta}tom5 yeast cells. The membrane-targeting mechanism of Tom5 appears to be distinct from that for proteins that are dispersed in the outer membrane.


Received for publication, July 2, 2003 , and in revised form, July 31, 2003.

* This work was supported by grants from the Ministry of Education, Science, and Culture of Japan (to M. S. and K. M.), from the Takeda Science Foundation, Core Research from Evolutional Science and Technology, and Specially Promoted Research from the Ministry of Education, Science, and Culture of Japan (to K. M.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} To whom correspondence should be addressed: Dept. of Molecular Biology, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan. Tel.: 81-92-642-6176; Fax: 81-92-642-6183; E-mail: mihara{at}cell.med.kyushu-u.ac.jp.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Cell Sci.Home page
C. Kemper, S. J. Habib, G. Engl, P. Heckmeyer, K. S. Dimmer, and D. Rapaport
Integration of tail-anchored proteins into the mitochondrial outer membrane does not require any known import components
J. Cell Sci., June 15, 2008; 121(12): 1990 - 1998.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Biol.Home page
D. Stojanovski, B. Guiard, V. Kozjak-Pavlovic, N. Pfanner, and C. Meisinger
Alternative function for the mitochondrial SAM complex in biogenesis of {alpha}-helical TOM proteins
J. Cell Biol., December 3, 2007; 179(5): 881 - 893.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Biol.Home page
A. Weber, S. A. Paschen, K. Heger, F. Wilfling, T. Frankenberg, H. Bauerschmitt, B. M. Seiffert, S. Kirschnek, H. Wagner, and G. Hacker
BimS-induced apoptosis requires mitochondrial localization but not interaction with anti-apoptotic Bcl-2 proteins
J. Cell Biol., May 21, 2007; 177(4): 625 - 636.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
E. L. Sherman, N. E. Go, and F. E. Nargang
Functions of the Small Proteins in the TOM Complex of Neurospora crasssa
Mol. Biol. Cell, September 1, 2005; 16(9): 4172 - 4182.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
C. Valentin, P. Dunoyer, G. Vetter, C. Schalk, A. Dietrich, and S. Bouzoubaa
Molecular Basis for Mitochondrial Localization of Viral Particles during Beet Necrotic Yellow Vein Virus Infection
J. Virol., August 1, 2005; 79(15): 9991 - 10002.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Schmitt, U. Ahting, L. Eichacker, B. Granvogl, N. E. Go, F. E. Nargang, W. Neupert, and S. Nussberger
Role of Tom5 in Maintaining the Structural Stability of the TOM Complex of Mitochondria
J. Biol. Chem., April 15, 2005; 280(15): 14499 - 14506.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
Y. T. Hwang, S. M. Pelitire, M. P.A. Henderson, D. W. Andrews, J. M. Dyer, and R. T. Mullen
Novel Targeting Signals Mediate the Sorting of Different Isoforms of the Tail-Anchored Membrane Protein Cytochrome b5 to Either Endoplasmic Reticulum or Mitochondria
PLANT CELL, November 1, 2004; 16(11): 3002 - 3019.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Esaki, H. Shimizu, T. Ono, H. Yamamoto, T. Kanamori, S.-i. Nishikawa, and T. Endo
Mitochondrial Protein Import: REQUIREMENT OF PRESEQUENCE ELEMENTS AND TOM COMPONENTS FOR PRECURSOR BINDING TO THE TOM COMPLEX
J. Biol. Chem., October 29, 2004; 279(44): 45701 - 45707.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Biol.Home page
R. L. Frederick, J. M. McCaffery, K. W. Cunningham, K. Okamoto, and J. M. Shaw
Yeast Miro GTPase, Gem1p, regulates mitochondrial morphology via a novel pathway
J. Cell Biol., October 11, 2004; 167(1): 87 - 98.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y. Nakamura, H. Suzuki, M. Sakaguchi, and K. Mihara
Targeting and Assembly of Rat Mitochondrial Translocase of Outer Membrane 22 (TOM22) into the TOM Complex
J. Biol. Chem., May 14, 2004; 279(20): 21223 - 21232.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.