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来自大肠杆菌的ATP合酶二环己基碳二亚胺结合蛋白c不足以表达高效的H⁺传导。

The dicyclohexylcarbodiimide-binding protein c of ATP synthase from Escherichia coli is not sufficient to express an efficient H+ conduction.

作者信息

Friedl P, Bienhaus G, Hoppe J, Schairer H U

出版信息

Proc Natl Acad Sci U S A. 1981 Nov;78(11):6643-6. doi: 10.1073/pnas.78.11.6643.

DOI:10.1073/pnas.78.11.6643
PMID:6273880
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC349105/
Abstract

Bacteriophage Mu was inserted into the unc genes of Escherichia coli. The resulting mutation AS12 had a polar effect on the unc operon: membranes of the mutant AS12 contained the dicyclohexylcarbodiimide-binding protein c and the protein a as sole subunits of the ATP synthase. It was shown by peptide mapping and amino acid analysis of the fragments that protein c from mutant AS12 was identical with the wild-type protein c. The absence of subunit b in mutant AS12 drastically lowered the H+ conduction dependent on the membrane-integrated moiety (F0) of the ATP synthase. This suggests that both subunits b and c are necessary for an efficient expression of H+ conduction.

摘要

噬菌体Mu被插入到大肠杆菌的unc基因中。产生的突变体AS12对unc操纵子有极性效应：突变体AS12的膜中含有二环己基碳二亚胺结合蛋白c和蛋白a作为ATP合酶的唯一亚基。通过对片段的肽图谱分析和氨基酸分析表明，突变体AS12的蛋白c与野生型蛋白c相同。突变体AS12中缺少亚基b极大地降低了依赖于ATP合酶膜整合部分（F0）的H+传导。这表明亚基b和c对于H+传导的有效表达都是必需的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c4/349105/cbe33ff9d14a/pnas00662-0107-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c4/349105/cbe33ff9d14a/pnas00662-0107-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/95c4/349105/cbe33ff9d14a/pnas00662-0107-a.jpg

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1
The dicyclohexylcarbodiimide-binding protein c of ATP synthase from Escherichia coli is not sufficient to express an efficient H+ conduction.来自大肠杆菌的ATP合酶二环己基碳二亚胺结合蛋白c不足以表达高效的H⁺传导。
Proc Natl Acad Sci U S A. 1981 Nov;78(11):6643-6. doi: 10.1073/pnas.78.11.6643.
2
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J Bacteriol. 1986 Jan;165(1):244-51. doi: 10.1128/jb.165.1.244-251.1986.
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Deletion of the gene for subunit III leads to defective assembly of bacterial cytochrome oxidase.亚基III基因的缺失导致细菌细胞色素氧化酶组装缺陷。
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Amino acid sequence of the proteolipid subunit of the proton-translocating ATPase complex from the thermophilic bacterium PS-3.嗜热细菌PS-3质子转运ATP酶复合体的蛋白脂质亚基的氨基酸序列。
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Interaction of [14C]dicyclohexylcarbodiimide with complex V (mitochondrial adenosine triphosphate synthetase complex).[14C]二环己基碳二亚胺与复合物V（线粒体腺苷三磷酸合成酶复合物）的相互作用。
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The proteolipid of a mutant ATPase from Escherichia coli defective in H+-conduction contains a glycine instead of the carbodiimide-reactive aspartyl residue.来自大肠杆菌的一种在质子传导方面存在缺陷的突变型ATP酶的蛋白脂质含有一个甘氨酸，而非碳二亚胺反应性天冬氨酰残基。
FEBS Lett. 1980 Jan 1;109(1):107-11. doi: 10.1016/0014-5793(80)81321-4.
8
The isolated F0 of Escherichia coli aTP-synthase is reconstitutively active in H+-conduction and ATP-dependent energy-transduction.大肠杆菌ATP合酶的分离F0在H⁺传导和ATP依赖的能量转导方面具有重组活性。
FEBS Lett. 1981 Jun 15;128(2):261-4. doi: 10.1016/0014-5793(81)80094-4.
9
Identification of amino-acid substitutions in the proteolipid subunit of the ATP synthase from dicyclohexylcarbodiimide-resistant mutants of Escherichia coli.从大肠杆菌二环己基碳二亚胺抗性突变体中鉴定ATP合酶蛋白脂质亚基中的氨基酸取代
Eur J Biochem. 1980 Nov;112(1):17-24. doi: 10.1111/j.1432-1033.1980.tb04981.x.
10
F0 of Escherichia coli ATP-synthase containing mutant and wild-type carbodiimide-binging proteins is impaired in H+ -conduction.含有突变型和野生型碳二亚胺结合蛋白的大肠杆菌ATP合酶的F0在H⁺传导方面受损。
FEBS Lett. 1980 Oct 6;119(2):254-6. doi: 10.1016/0014-5793(80)80265-1.