Pam16 has an essential role in the mitochondrial protein import motor

被引：158
作者：
Frazier, AE
Dudek, J
Guiard, B
Voos, W
Li, YF
Lind, M
Meisinger, C
Geissler, A
Sickmann, A
Meyer, HE
Bilanchone, V
Cumsky, MG
Truscott, KN
Pfanner, N
Rehling, P
机构：
[1] Univ Freiburg, Inst Biochem & Mol Biol, D-79104 Freiburg, Germany
[2] Univ Freiburg, Fak Biol, D-79104 Freiburg, Germany
[3] Univ Paris 06, CNRS, Lab Propre, F-91190 Gif Sur Yvette, France
[4] Ruhr Univ Bochum, Med Proteom Ctr, D-44780 Bochum, Germany
[5] Univ Wurzburg, Rudolf Virchow Ctr Expt Biomed, D-97078 Wurzburg, Germany
[6] Univ Calif Irvine, Dept Mol Biol & Biochem, Irvine, CA 92697 USA
来源：
NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2004年 / 11卷 / 03期
关键词：
D O I：
10.1038/nsmb735
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Mitochondrial preproteins destined for the matrix are translocated by two channel-forming transport machineries, the translocase of the outer membrane and the presequence translocase of the inner membrane. The presequence translocase-associated protein import motor (PAM) contains four essential subunits: the matrix heat shock protein 70 (mtHsp70) and its three cochaperones Mge1, Tim44 and Pam18. Here we report that the PAM contains a fifth essential subunit, Pam16 ( encoded by Saccharomyces cerevisiae YJL104W), which is selectively required for preprotein translocation into the matrix, but not for protein insertion into the inner membrane. Pam16 interacts with Pam18 and is needed for the association of Pam18 with the presequence translocase and for formation of a mtHsp70 Tim44 complex. Thus, Pam16 is a newly identified type of motor subunit and is required to promote a functional PAM reaction cycle, thereby driving preprotein import into the matrix.
引用
收藏
页码：226 / 233
页数：8
相关论文
共 51 条
[1]   Two distinct and independent mitochondrial targeting signals function in the sorting of an inner membrane protein, cytochrome c1 [J].
Arnold, I ;
Fölsch, H ;
Neupert, W ;
Stuart, RA .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (03) :1469-1476
[2]   Role of Tim23 as voltage sensor and presequence receptor in protein import into mitochondria [J].
Bauer, MF ;
Sirrenberg, C ;
Neupert, W ;
Brunner, M .
CELL, 1996, 87 (01) :33-41
[3]   Protein translocation into mitochondria: the role of TIM complexes [J].
Bauer, MF ;
Hofmann, S ;
Neupert, W ;
Brunner, M .
TRENDS IN CELL BIOLOGY, 2000, 10 (01) :25-31
[4]   The black-pearl gene of Drosophila defines a novel conserved protein family and is required for larval growth and survival [J].
Becker, S ;
Gehrsitz, A ;
Bork, P ;
Buchner, S ;
Buchner, E .
GENE, 2001, 262 (1-2) :15-22
[5]  
BORNER U, 1998, EMBO J, V17, P4226
[6]   The Hsp70 and Hsp60 chaperone machines [J].
Bukau, B ;
Horwich, AL .
CELL, 1998, 92 (03) :351-366
[7]   Mitochondrial translocation contact sites: separation of dynamic and stabilizing elements in formation of a TOM-TIM-preprotein supercomplex [J].
Chacinska, A ;
Rehling, P ;
Guiard, B ;
Frazier, AE ;
Schulze-Specking, A ;
Pfanner, N ;
Voos, W ;
Meisinger, C .
EMBO JOURNAL, 2003, 22 (20) :5370-5381
[8]   J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix [J].
D'Silva, PD ;
Schilke, B ;
Walter, W ;
Andrew, A ;
Craig, EA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (24) :13839-13844
[9]   The Tim core complex defines the number of mitochondrial translocation contact sites and can hold arrested preproteins in the absence of matrix Hsp70-Tim44 [J].
Dekker, PJT ;
Martin, F ;
Maarse, AC ;
Bomer, U ;
Muller, H ;
Guiard, B ;
Meijer, M ;
Rassow, J ;
Pfanner, N .
EMBO JOURNAL, 1997, 16 (17) :5408-5419
[10]   Functions of outer membrane receptors in mitochondrial protein import [J].
Endo, T ;
Kohda, D .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2002, 1592 (01) :3-14
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