The mitochondrial import receptor Tom70: Identification of a 25 kDa core domain with a specific binding site for preproteins

被引:74
作者
Brix, J
Ziegler, GA
Dietmeier, K
Schneider-Mergener, J
Schulz, GE
Pfanner, N
机构
[1] Univ Freiburg, Inst Biochem & Mol Biol, D-79104 Freiburg, Germany
[2] Univ Freiburg, Inst Organ Chem & Biochem, D-79104 Freiburg, Germany
[3] Humboldt Univ, Inst Med Immunol, Klinikum Charite, D-10098 Berlin, Germany
关键词
import receptor; mitochondria; protein sorting; Saccharomyces cerevisiae; Tom70;
D O I
10.1006/jmbi.2000.4120
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
The mitochondrial import receptor of 70 kDa, Tom70, preferentially recognizes precursors of membrane proteins with internal targeting signals. We report the identification of a stably folded 25 kDa core domain located in the middle portion of Tom70 that contains two of the seven tetratricopeptide repeat motifs of the receptor. The core domain binds non-cleavable and cleavable preproteins carrying internal targeting signals with a specificity indistinguishable from the full-length receptor. Competition studies indicate that both types of preproteins interact with overlapping binding sites of the core domain and that at least one additional interaction site is present in the full-length receptor. We suggest a model of Tom70 function in import of membrane proteins whereby a hydrophobic preprotein concomitantly interacts with several binding sites of the receptor. (C) 2000 Academic Press.
引用
收藏
页码:479 / 488
页数:10
相关论文
共 41 条
[1]   Structural basis of presequence recognition by the mitochondrial protein import receptor Tom20 [J].
Abe, Y ;
Shodai, T ;
Muto, T ;
Mihara, K ;
Torii, H ;
Nishikawa, S ;
Endo, T ;
Kohda, D .
CELL, 2000, 100 (05) :551-560
[2]   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
[3]   Acidic receptor domains on both sides of the outer membrane mediate translocation of precursor proteins into yeast mitochondria [J].
Bolliger, L ;
Junne, T ;
Schatz, G ;
Lithgow, T .
EMBO JOURNAL, 1995, 14 (24) :6318-6326
[4]   Differential recognition of preproteins by the purified cytosolic domains of the mitochondrial import receptors Tom20, Tom22, and Tom70 [J].
Brix, J ;
Dietmeier, K ;
Pfanner, N .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (33) :20730-20735
[5]   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, J ;
Rüdiger, S ;
Bukau, B ;
Schneider-Mergener, J ;
Pfanner, N .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (23) :16522-16530
[6]   The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions [J].
Das, AK ;
Cohen, PTW ;
Barford, D .
EMBO JOURNAL, 1998, 17 (05) :1192-1199
[7]  
DAUM G, 1982, J BIOL CHEM, V257, P3028
[8]   Role of mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70 [J].
Dekker, PJT ;
Pfanner, N .
JOURNAL OF MOLECULAR BIOLOGY, 1997, 270 (03) :321-327
[9]   Transport of the ADP ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex [J].
Endres, M ;
Neupert, W ;
Brunner, M .
EMBO JOURNAL, 1999, 18 (12) :3214-3221
[10]   A DUAL ROLE FOR MITOCHONDRIAL HEAT-SHOCK PROTEIN-70 IN MEMBRANE TRANSLOCATION OF PREPROTEINS [J].
GAMBILL, BD ;
VOOS, W ;
KANG, PJ ;
MIAO, BJ ;
LANGER, T ;
CRAIG, EA ;
PFANNER, N .
JOURNAL OF CELL BIOLOGY, 1993, 123 (01) :109-117