The second stalk of Escherichia coli ATP synthase

被引:77
作者
Dunn, SD [1 ]
McLachlin, DT [1 ]
Revington, M [1 ]
机构
[1] Univ Western Ontario, Dept Biochem, London, ON N6A 5C1, Canada
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2000年 / 1458卷 / 2-3期
基金
英国医学研究理事会;
关键词
adenosine triphosphate synthase; stator; b subunit; delta subunit; stalk;
D O I
10.1016/S0005-2728(00)00086-4
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
Two stalks link the F-1 and F-0 sectors of ATP synthase. The central stalk contains the gamma and epsilon subunits and is thought to function in rotational catalysis as a rotor driving conformational changes in the catalytic alpha(3)beta(3) complex. The two b subunits and the delta subunit associate to form b(2)delta, a second, peripheral stalk extending from the membrane up the side of alpha(3)beta(3) and binding to the N-terminal regions of the a subunits, which are approx. 125 Angstrom from the membrane. This second stalk is essential for binding F-1 to F-0 and is believed to function as a stator during rotational catalysis. In vitro, b(2)delta is a highly extended complex held together by weak interactions. Recent work has identified the domains of b which are essential for dimerization and for interaction with delta. Disulphide cross-linking studies imply that the second stalk is a permanent structure which remains associated with one alpha subunit or alpha beta pair. However, the weak interactions between the polypeptides in b2 delta pose a challenge for the proposed stator function. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:356 / 363
页数:8
相关论文
共 50 条
[1]   STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].
ABRAHAMS, JP ;
LESLIE, AGW ;
LUTTER, R ;
WALKER, JE .
NATURE, 1994, 370 (6491) :621-628
[2]  
ARIS JP, 1983, J BIOL CHEM, V258, P4599
[3]   ZERO-LENGTH CROSS-LINKING BETWEEN SUBUNITS DELTA AND I OF THE H+-TRANSLOCATING ATPASE OF CHLOROPLASTS [J].
BECKERS, G ;
BERZBORN, RJ ;
STROTMANN, H .
BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1101 (01) :97-104
[4]   The ATP synthase - A splendid molecular machine [J].
Boyer, PD .
ANNUAL REVIEW OF BIOCHEMISTRY, 1997, 66 :717-749
[5]   THE BINDING CHANGE MECHANISM FOR ATP SYNTHASE - SOME PROBABILITIES AND POSSIBILITIES [J].
BOYER, PD .
BIOCHIMICA ET BIOPHYSICA ACTA, 1993, 1140 (03) :215-250
[6]   Identification of an uncoupling mutation affecting the b subunit of F1F0 ATP synthase in Escherichia coli [J].
Caviston, TL ;
Ketchum, CJ ;
Sorgen, PL ;
Nakamoto, RK ;
Cain, BD .
FEBS LETTERS, 1998, 429 (02) :201-206
[7]   Transient accumulation of elastic energy in proton translocating ATP synthase [J].
Cherepanov, DA ;
Mulkidjanian, AY ;
Junge, W .
FEBS LETTERS, 1999, 449 (01) :1-6
[8]  
COLLINSON IR, 1994, J MOL BIOL, V242, P408
[9]   Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase [J].
Dmitriev, O ;
Jones, PC ;
Jiang, WP ;
Fillingame, RH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (22) :15598-15604
[10]  
DUNN SD, 1980, J BIOL CHEM, V255, P6891