SUBSTITUTION OF THE CYSTEINYL RESIDUE (CYS21) OF SUBUNIT-B OF THE ATP SYNTHASE FROM ESCHERICHIA-COLI

被引：5

作者：

KAUFFER, S ^{[1
]}

DECKERSHEBESTREIT, G ^{[1
]}

ALTENDORF, K ^{[1
]}

机构：

[1] UNIV OSNABRUCK,FACHBEREICH BIOL CHEM,ARBEITSGRP MIKROBIOL,BARBARASTR 11,W-4500 OSNABRUCK,GERMANY

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1991年 / 202卷 / 03期

关键词：

D O I：

10.1111/j.1432-1033.1991.tb16504.x

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：

The F(o) complex of the ATP synthase (F1F(o)) of Escherichia coli contains only two cysteinyl residues, Cys21, of the two copies of subunit b. Modification of Cys21 with the hydrophobic maleimide N-(7-dimethylamino-4-methyl-coumarinyl)maleimide resulted in impairment of F(o) functions [Schneider, E. & Altendorf, K. (1985) Eur. J. Biochem. 153, 105-109]. We replaced this residue (via cassette mutagenesis) by Ser, Gly, Ala, Thr, Asp and Pro. None of the replacements resulted in detectable alterations of the function of the ATP synthase, making a functional role for these sulfhydryl residues unlikely. Due to its high tolerance towards amino acid substitutions, the region around Cys21 seems not to be a protein-protein contact area.

引用

页码：1307 / 1312

页数：6

共 56 条

[1] AUTOMATED CONTINUOUS ASSAY OF MEMBRANE-BOUND AND SOLUBLE ATPASES AND RELATED ENZYMES [J].