GENE DUPLICATION AS A MEANS FOR ALTERING H+/ATP RATIOS DURING THE EVOLUTION OF F0F1 ATPASES AND SYNTHASES

被引:63
作者
CROSS, RL [1 ]
TAIZ, L [1 ]
机构
[1] UNIV CALIF SANTA CRUZ,SANTA CRUZ,CA 95064
关键词
ATP synthase; Evolution; Gene duplication; H[!sup]+[!/sup]/ATP-ratios; Proton-translocating ATPase;
D O I
10.1016/0014-5793(90)80014-A
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
In the evolution of the FoF1 family of proton-translocating membrane complexes, two reversals in function appear to have occurred, first changing it from an ATPase to an ATP synthase and then back again to an ATPase. Here we suggest that with each change in function, the ratio of protons transported per ATP hydrolyzed or synthesized (H+/ATP) was altered in order for the complex to better adapt to its new role. We propose that this was accomplished by gene duplication with partial loss in the number of functional catalytic sites (to increase H+/ATP) or functional proton channels (to decrease H+/ATP). This method of changing the H+/ATP ratio preserved overall structural features of the complex essential to energy coupling. © 1990.
引用
收藏
页码:227 / 229
页数:3
相关论文
共 22 条
[1]  
ARAI H, 1988, J BIOL CHEM, V263, P8796
[2]   H+-ATPASE ACTIVITY FROM STORAGE TISSUE OF BETA-VULGARIS .2. H+-ATP STOICHIOMETRY OF AN ANION-SENSITIVE H+-ATPASE [J].
BENNETT, AB ;
SPANSWICK, RM .
PLANT PHYSIOLOGY, 1984, 74 (03) :545-548
[3]  
BERRY EA, 1983, J BIOL CHEM, V258, P1474
[4]  
CROSS RL, 1982, J BIOL CHEM, V257, P2874
[5]  
DENDA K, 1988, J BIOL CHEM, V263, P6012
[6]  
ESCH FS, 1979, J BIOL CHEM, V254, P740
[7]   STRUCTURE AND FUNCTION OF VACUOLAR CLASS OF ATP-DRIVEN PROTON PUMPS [J].
FORGAC, M .
PHYSIOLOGICAL REVIEWS, 1989, 69 (03) :765-796
[8]  
FOSTER DL, 1982, J BIOL CHEM, V257, P2009
[9]   EVOLUTION OF THE VACUOLAR H+-ATPASE - IMPLICATIONS FOR THE ORIGIN OF EUKARYOTES [J].
GOGARTEN, JP ;
KIBAK, H ;
DITTRICH, P ;
TAIZ, L ;
BOWMAN, EJ ;
BOWMAN, BJ ;
MANOLSON, MF ;
POOLE, RJ ;
DATE, T ;
OSHIMA, T ;
KONISHI, J ;
DENDA, K ;
YOSHIDA, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1989, 86 (17) :6661-6665
[10]   PROTEOLIPID OF A MUTANT ATPASE FROM ESCHERICHIA-COLI DEFECTIVE IN H+-CONDUCTION CONTAINS A GLYCINE INSTEAD OF THE CARBODIIMIDE-REACTIVE ASPARTYL RESIDUE [J].
HOPPE, J ;
SCHAIRER, HU ;
SEBALD, W .
FEBS LETTERS, 1980, 109 (01) :107-111