ESCHERICHIA-COLI RUVA AND RUVB PROTEINS INVOLVED IN RECOMBINATION REPAIR - PHYSICAL-PROPERTIES AND INTERACTIONS WITH DNA

被引：45

作者：

SHIBA, T ^{[1
]}

IWASAKI, H ^{[1
]}

NAKATA, A ^{[1
]}

SHINAGAWA, H ^{[1
]}

机构：

[1] OSAKA UNIV,MICROBIAL DIS RES INST,DEPT EXPTL CHEMOTHERAPY,SUITA,OSAKA 565,JAPAN

来源：

MOLECULAR & GENERAL GENETICS | 1993年 / 237卷 / 03期

关键词：

ATPASE; DNA BINDING PROTEIN; HOLLIDAY JUNCTION; RECOMBINATION; SUBUNIT STRUCTURE;

D O I：

10.1007/BF00279443

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：

Escherichia coli RuvA and RuvB proteins are encoded by an SOS-regulated operon, which is involved in DNA repair and recombination. RuvB has weak ATPase activity, which is enhanced by the addition of RuvA and DNA, and RuvA and RuvB in the presence of ATP promote branch migration at Holliday junctions. In this work, the physical states of RuvA and RuvB and their interactions with DNA were studied by sedimentation analysis and gel filtration chromatography. RuvA formed a stable tetramer in solution, which resisted dissociation by SDS at room temperature. RuvB formed a dimer in solution. When RuvA and RuvB were mixed, an oligomer complex was formed consisting of a tetrameric form of RuvA and a dimeric form of RuvB, and this complex bound to DNA. The maximal enhancement of the RuvB ATPase activity by RuvA was achieved at this stoichiometry in the presence of excess DNA.

引用

页码：395 / 399

页数：5

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