HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 281, Issue 1, 36-42, January 6, 2006

This Article Full Text Full Text (PDF) All Versions of this Article: 281/1/36    most recent M509819200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Matsuzono, Y. Articles by Fujiki, Y. Search for Related Content PubMed PubMed Citation Articles by Matsuzono, Y. Articles by Fujiki, Y. Social Bookmarking                      What's this?

In Vitro Transport of Membrane Proteins to Peroxisomes by Shuttling Receptor Pex19p^*

Yuji Matsuzono and Yukio Fujiki1

From the Department of Biology, Faculty of Sciences, Kyushu University Graduate School, Fukuoka 812-8581, Japan and SORST, Japan Science and Technology Agency, Kawaguchi, Saitama 332-0012, Japan

The peroxin Pex19p comprising 299 amino acids functions in peroxisomal membrane assembly. We here developed a cell-free system for transport of membrane proteins to peroxisomes. Pex19p interacts with multiple membrane peroxins, including other membrane biogenesis peroxins, Pex16p and Pex26p, involved in matrix protein import. Cell-free synthesized, ³⁵S-labeled Pex19p was targeted to subcellular fractions containing peroxisomes from Chinese hamster ovary-K1 cells as well as peroxisomes isolated from rat liver in an ATP-dependent manner. Such translocation was also reproduced with in vitro synthesized ³⁵S-Pex16p with two transmembrane segments and C-tail anchor-type ³⁵S-Pex26p, upon incubation with ³⁵S-Pex19p in the reaction mixtures containing isolated peroxisomes. The transported ³⁵S-Pex16p and ³⁵S-Pex26p were integrated into membranes as assessed by the sodium carbonate extraction method. Peroxisome-associated and partly Na₂CO₃-resistant ³⁵S-Pex19p was released to the cytosolic fraction upon incubation in the absence of ATP, whereas ³⁵S-Pex16p and ³⁵S-Pex26p remained in the membranes. Furthermore, not only ³⁵S-Pex19p but also ³⁵S-Pex19p complexes each with ³⁵S-Pex16p and ³⁵S-Pex26p were bound to ³⁵S-Pex3p in vitro. Together, these results strongly suggested that Pex19p translocates the membrane peroxins from the cytosol to peroxisomes in an ATP- and Pex3p-dependent manner and then shuttles back to the cytosol.

Received for publication, September 7, 2005 , and in revised form, October 24, 2005.

^* This work was supported in part by a SORST grant from the Science and Technology Agency of Japan (to Y. F.), grants-in-aid for scientific research (to Y .F.) from National Project on Protein Structural and Functional Analyses (to Y. F.), and grants from The 21st Century COE Program from The Ministry of Education, Culture, Sports, Science, and Technology of Japan, the Uehara Memorial Foundation (to Y.F.), Japan Foundation for Applied Enzymology, and Takeda Science Foundation. 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.

¹ To whom correspondence should be addressed: Dept. of Biology, Faulty of Sciences, Kyushu University Graduate School, 6-10-1 Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan. Tel.: 81-92-642-2635; Fax: 81-92-642-4214; E-mail: yfujiscb{at}mbox.nc.kyushu-u.ac.jp.

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

This article has been cited by other articles:

				E. H. Hettema and A. M. Motley How peroxisomes multiply J. Cell Sci., July 15, 2009; 122(14): 2331 - 2336. [Abstract] [Full Text] [PDF]

				A. Halbach, R. Rucktaschel, H. Rottensteiner, and R. Erdmann The N-domain of Pex22p Can Functionally Replace the Pex3p N-domain in Targeting and Peroxisome Formation J. Biol. Chem., February 6, 2009; 284(6): 3906 - 3916. [Abstract] [Full Text] [PDF]

				T. Matsuzaki and Y. Fujiki The peroxisomal membrane protein import receptor Pex3p is directly transported to peroxisomes by a novel Pex19p- and Pex16p-dependent pathway J. Cell Biol., December 29, 2008; 183(7): 1275 - 1286. [Abstract] [Full Text] [PDF]

				Y. Sato, H. Shibata, H. Nakano, Y. Matsuzono, Y. Kashiwayama, Y. Kobayashi, Y. Fujiki, T. Imanaka, and H. Kato Characterization of the Interaction between Recombinant Human Peroxin Pex3p and Pex19p: IDENTIFICATION OF TRP-104 IN Pex3p AS A CRITICAL RESIDUE FOR THE INTERACTION J. Biol. Chem., March 7, 2008; 283(10): 6136 - 6144. [Abstract] [Full Text] [PDF]

				T. Saveria, A. Halbach, R. Erdmann, R. Volkmer-Engert, C. Landgraf, H. Rottensteiner, and M. Parsons Conservation of PEX19-Binding Motifs Required for Protein Targeting to Mammalian Peroxisomal and Trypanosome Glycosomal Membranes Eukaryot. Cell, August 1, 2007; 6(8): 1439 - 1449. [Abstract] [Full Text] [PDF]

				M. P. Pinto, C. P. Grou, I. S. Alencastre, M. E. Oliveira, C. Sa-Miranda, M. Fransen, and J. E. Azevedo The Import Competence of a Peroxisomal Membrane Protein Is Determined by Pex19p before the Docking Step J. Biol. Chem., November 10, 2006; 281(45): 34492 - 34502. [Abstract] [Full Text] [PDF]

				Y. Matsuzono, T. Matsuzaki, and Y. Fujiki Functional domain mapping of peroxin Pex19p: interaction with Pex3p is essential for function and translocation J. Cell Sci., September 1, 2006; 119(17): 3539 - 3550. [Abstract] [Full Text] [PDF]

				R. Itoh and Y. Fujiki Functional Domains and Dynamic Assembly of the Peroxin Pex14p, the Entry Site of Matrix Proteins J. Biol. Chem., April 14, 2006; 281(15): 10196 - 10205. [Abstract] [Full Text] [PDF]