Toc12, a novel subunit of the intermembrane space preprotein translocon of chloroplasts

被引:78
作者
Becker, T
Hritz, J
Vogel, M
Caliebe, A
Bukau, B
Soll, J
Schleiff, E [1 ]
机构
[1] Univ Munich, Inst Bot, D-80638 Munich, Germany
[2] PJ Safaik Univ, Dept Biophys, Kosice 04154, Slovakia
[3] Heidelberg Univ, Zentrum Mol Biol, D-69120 Heidelberg, Germany
[4] Univ Kiel, Inst Bot, D-24118 Kiel, Germany
关键词
D O I
10.1091/mbc.E04-05-0405
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Translocation of proteins across membranes is essential for the biogenesis of each cell and is achieved by proteinaceous complexes. We analyzed the translocation complex of the intermembrane space from chloroplasts and identified a 12-kDa protein associated with the Toc machinery. Toc12 is an outer envelope protein exposing a soluble domain into the intermembrane space. Toc12 contains a J-domain and stimulates the ATPase activity of DnaK. The conformational stability and the ability to stimulate Hsp70 are dependent on a disulfide bridge within the loop region of the J-domain, suggesting a redox-regulated activation of the chaperone. Toc12 is associated with Toc64 and Tic22. Its J-domain recruits the Hsp70 of outer envelope membrane to the intermembrane space translocon and facilitates its interaction to the preprotein.
引用
收藏
页码:5130 / 5144
页数:15
相关论文
共 75 条
[71]   Phosphorylation of the transit sequence of chloroplast precursor proteins [J].
Waegemann, K ;
Soll, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (11) :6545-6554
[72]   THE CONSERVED G/F MOTIF OF THE DNAJ CHAPERONE IS NECESSARY FOR THE ACTIVATION OF THE SUBSTRATE-BINDING PROPERTIES OF THE DNAK CHAPERONE [J].
WALL, D ;
ZYLICZ, M ;
GEORGOPOULOS, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (05) :2139-2144
[73]   Designing transmembrane α-helices that insert spontaneously [J].
Wimley, WC ;
White, SH .
BIOCHEMISTRY, 2000, 39 (15) :4432-4442
[74]  
WU CB, 1994, J BIOL CHEM, V269, P32264
[75]  
ZYLICZ M, 1985, J BIOL CHEM, V260, P7591