RecR is a zinc metalloprotein from Bacillus subtilis 168

被引:10
作者
Ayora, S
Stiege, AC
Alonso, JC
机构
[1] UNIV AUTONOMA MADRID,CSIC,CTR NACL BIOTECNOL,E-28049 MADRID,SPAIN
[2] MAX PLANCK INST MOL GENET,D-14195 BERLIN,GERMANY
关键词
D O I
10.1046/j.1365-2958.1997.2431611.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 Bacillus subtilis RecR protein is required for DNA repair and recombination in vivo. In its N-terminal portion, RecR possesses potential zinc-ligand structures associated with the multicysteine (C-4) superfamily. The number and arrangement of the cysteine residues is suggestive of RecR being a-zinc-finger protein. One of the four cysteines (Cys-60) has been replaced by a Ser (C60S) or an Ala (C60A) residue to generate the recR60 and recRG01 genes, respectively. B. subtilis recR60, recRG01 or Delta recR1 (a null-mutant allele) cells are 10-, 134- and 144-fold more sensitive to 10 mM methanesulphonate and 95-, 900- and 1100-fold more sensitive to the lethal effect of 100 mu M 4-nitroquinoline-1-oxide (4NQO) than the wild-type strain, respectively. The RecR zinc-ligand C-4 motif does not seem to be accessible, because the protein is highly resistant to oxidation and moderately resistant to reduction. We have determined by different biochemical methods that RecR is a zinc metalloprotein whose cysteine residues have a structural and/or functional role.
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收藏
页码:639 / 647
页数:9
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