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通过特异性去除CF0多肽推导叶绿体ATP合酶(CF0-CF1)内的亚基相互作用

Subunit interactions within the chloroplast ATP synthase (CF0-CF1) as deduced by specific depletion of CF0 polypeptides.

作者信息

Feng Y, McCarty R E

机构信息

Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853.

出版信息

J Biol Chem. 1990 Jul 25;265(21):12481-5.

PMID:2142688
Abstract

The proton-linked ATP synthase (CF1-CF0) of chloroplasts consists of a catalytic component (CF1) and a membrane-embedded part (CF0) that interacts with CF1 and contains a proton channel. The subunits of CF0 which are involved in binding of CF1 were studied by examining the effect of selective depletion of subunits I, II, and IV of CF0 from the chloroplast ATP synthase on the association of the remaining CF0 subunits with CF1. Dissociated CF0 subunits were identified by sucrose density gradient centrifugation. Removal of subunit IV alone from CF0-CF1 did not cause dissociation of the other CF0 subunits from CF1. Upon removal of both subunits I and IV from CF0-CF1, subunit II also dissociated, but subunit III was still bound to CF1. Thus, at least two subunits of CF0, I and III, directly associate with CF1. Subunit II is unlikely to bind CF1 directly and may associate with subunit I. Although depletion of subunit IV does not cause dissociation of CF0 from CF1, its interaction with CF1 subunits is uncertain.

摘要

叶绿体的质子偶联ATP合酶(CF1 - CF0)由催化组分(CF1)和膜嵌入部分(CF0)组成,CF0与CF1相互作用并包含一个质子通道。通过研究从叶绿体ATP合酶中选择性去除CF0的亚基I、II和IV对其余CF0亚基与CF1结合的影响,对参与CF1结合的CF0亚基进行了研究。通过蔗糖密度梯度离心鉴定解离的CF0亚基。仅从CF0 - CF1中去除亚基IV不会导致其他CF0亚基与CF1解离。当从CF0 - CF1中同时去除亚基I和IV时,亚基II也会解离,但亚基III仍与CF1结合。因此,CF0至少有两个亚基,即I和III,直接与CF1结合。亚基II不太可能直接结合CF1,可能与亚基I结合。虽然亚基IV的缺失不会导致CF0与CF1解离,但其与CF1亚基的相互作用尚不确定。

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