Direct interaction between a membrane domain subunit and a connector subunit in the H+-translocating NADH-quinone oxidoreductase

被引:26
作者
Di Bernardo, S [1 ]
Yagi, T [1 ]
机构
[1] Scripps Res Inst, Dept Mol & Expt Med, Div Biochem, La Jolla, CA 92037 USA
关键词
NADH dehydrogenase; subunit crosslink; proton pump; iron-sulfur clusters; bacterial proton-translocating NADH-quinone oxidoreductase; Paracoccus denitrificans;
D O I
10.1016/S0014-5793(01)03111-8
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
When Paracoccus denitrificans membranes were treated with a crosslinker, m-maleimidobenzoyl-N-hydroxysuccinimide ester (MBS), a cross-linked product of M-r similar to 31 kDa was found which reacted with antibodies against the hydrophobic subunit Nqo7 and the connector subunit Nqo6. NaI treatment of the Paracoccus membranes before, but not after, the crosslinking step prevented the formation of the 31 kDa band. When Nqo7 and Nqo6 were coexpressed in Escherichia coli, both subunits were located in the membrane fraction. NIBS treatment of the E. coli membranes generated the 31 kDa band as in the Paracoccus membranes. These results indicate that Nqo7 interacts with probable N2-binding Nqo6. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:385 / 388
页数:4
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