Dimeric H+-ATP synthase in the chloroplast of Chlamydomonas reinhardtii

被引:51
作者
Rexroth, S [1 ]
Tittingdorf, RMWMZ [1 ]
Schwassmann, HJ [1 ]
Krause, F [1 ]
Seelert, H [1 ]
Dencher, NA [1 ]
机构
[1] TH Darmstadt, Dept Chem, D-64287 Darmstadt, Germany
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2004年 / 1658卷 / 03期
关键词
chloroplast ATP synthase; blue-native electrophoresis; Chlamydomonas reinhardtii; membrane protein complex; thylakoid membrane;
D O I
10.1016/j.bbabio.2004.05.014
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
H+-ATP synthase is the dominant ATP production site in mitochondria and chloroplasts. So far, dimerization of ATP synthase has been observed only in mitochondria by biochemical and electron microscopic investigations. Although the physiological relevance remains still enigmatic, dimerization was proposed to be a unique feature of the mitochondrion [Biochim. Biophys. Acta 1555 (2002) 154]. It is hard to imagine, however, that closely related protein complexes of mitochondria and chloroplast should show such severe differences in structural organization. We present the first evidences for dimerization of chloroplast ATP synthases within the thylakoid membrane. By investigation of the thylakoid membrane of Chlamydomonas reinhardtii by blue-native polyacrylamide gel electrophoresis, dimerization of the chloroplast ATP synthase was detected. Chloroplast ATP synthase dimer dissociates into monomers upon incubation with vanadate or phosphate but not by incubation with molybdate, while the mitochondrial dimer is not affected by the incubation. This suggests a distinct dimerization mechanism for mitochondrial and chloroplast ATP synthase. Since vanadate and phosphate bind to the active sites, contact sites located on the hydrophilic CF1 part are suggested for the chloroplast ATP synthase dimer. As the degree of dimerization varies with phosphate concentration, dimerization might be a response to low phosphate concentrations. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:202 / 211
页数:10
相关论文
共 46 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]   AN INVESTIGATION OF MITOCHONDRIAL INNER MEMBRANES BY RAPID-FREEZE DEEP-ETCH TECHNIQUES [J].
ALLEN, RD ;
SCHROEDER, CC ;
FOK, AK .
JOURNAL OF CELL BIOLOGY, 1989, 108 (06) :2233-2240
[3]   Insights into the consequences of grana stacking of thylakoid membranes in vascular plants: a personal perspective [J].
Anderson, JM .
AUSTRALIAN JOURNAL OF PLANT PHYSIOLOGY, 1999, 26 (07) :625-639
[4]   Yeast mitochondrial F1F0-ATP synthase exists as a dimer:: identification of three dimer-specific subunits [J].
Arnold, I ;
Pfeiffer, K ;
Neupert, W ;
Stuart, RA ;
Schägger, H .
EMBO JOURNAL, 1998, 17 (24) :7170-7178
[5]   IMPROVED SILVER STAINING OF PLANT-PROTEINS, RNA AND DNA IN POLYACRYLAMIDE GELS [J].
BLUM, H ;
BEIER, H ;
GROSS, HJ .
ELECTROPHORESIS, 1987, 8 (02) :93-99
[6]   The structure of the H+-ATP synthase from chloroplasts and its subcomplexes as revealed by electron microscopy [J].
Böttcher, B ;
Gräber, P .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2000, 1458 (2-3) :404-416
[7]   THE BINDING CHANGE MECHANISM FOR ATP SYNTHASE - SOME PROBABILITIES AND POSSIBILITIES [J].
BOYER, PD .
BIOCHIMICA ET BIOPHYSICA ACTA, 1993, 1140 (03) :215-250
[8]   Dimerization of bovine F1-ATPase by binding the inhibitor protein, IF1 [J].
Cabezón, E ;
Arechaga, I ;
Butler, PJG ;
Walker, JE .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (37) :28353-28355
[9]   ATP synthase: A tentative structural model [J].
Engelbrecht, S ;
Junge, W .
FEBS LETTERS, 1997, 414 (03) :485-491
[10]   New insights into the respiratory chain of plant mitochondria.: Supercomplexes and a unique composition of complex II [J].
Eubel, H ;
Jänsch, L ;
Braun, HP .
PLANT PHYSIOLOGY, 2003, 133 (01) :274-286