F0 AND F1 PARTS OF ATP SYNTHASES FROM CLOSTRIDIUM-THERMOAUTOTROPHICUM AND ESCHERICHIA-COLI ARE NOT FUNCTIONALLY COMPATIBLE

被引：7

作者：

DAS, A

LJUNGDAHL, LG

机构：

[1] UNIV GEORGIA,CTR BIOL RESOURCE RECOVERY,ATHENS,GA 30602

[2] UNIV GEORGIA,DEPT BIOCHEM,ATHENS,GA 30602

来源：

FEBS LETTERS | 1993年 / 317卷 / 1-2期

关键词：

CLOSTRIDIUM-THERMOAUTOTROPHICUM; ESCHERICHIA-COLI; F1F0-ATP SYNTHASE; INVITRO RECONSTITUTION; FUNCTIONAL COMPATIBILITY;

D O I：

10.1016/0014-5793(93)81482-F

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：

F1-stripped membrane vesicles from Clostridium thermoautotrophicum and Escherichia coli were reconstituted with F1-ATPases from both bacteria. Reconstituted F1F0-ATPase complexes were catalytically active, i.e. capable of hydrolyzing ATP. Homologous-type ATPase complexes having F0 and F1 parts of ATP synthases from the same origin were DCCD sensitive and supported ATP-driven enhancement of anilinonaphthalene sulfonate (ANS) fluorescence. Hybrid-type ATPase complexes having F0 and F1 parts of ATP synthases from different origins were neither DCCD sensitive nor did they support ATP-driven enhancement of ANS fluorescence. Analyzing these results it has been demonstrated that the F0 and F1 parts of ATP synthases of these two bacteria are not functionally compatible.

引用

页码：17 / 21

页数：5

共 26 条

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