HOMOLOGOUS PAIRING OF SINGLE-STRANDED-DNA AND SUPERHELICAL DOUBLE-STRANDED DNA CATALYZED BY RECO PROTEIN FROM ESCHERICHIA-COLI
HOMOLOGOUS PAIRING OF SINGLE-STRANDED-DNA AND SUPERHELICAL DOUBLE-STRANDED DNA CATALYZED BY RECO PROTEIN FROM ESCHERICHIA-COLI
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DOI：
10.1128/jb.177.3.566-572.1995
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发表时间：
1995-02-01
影响因子：
3.2
通讯作者：
LUISIDELUCA, C
中科院分区：
文献类型：
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作者：
LUISIDELUCA, C
recO基因产物是野生型大肠杆菌细胞中DNA修复和某些类型同源重组所必需的。RecO蛋白先前已被纯化，并显示结合到单链和双链DNA，并促进互补单链DNA分子的复性。在这项研究中，纯化的RecO蛋白被证明可以催化单链DNA同化成同源超螺旋双链DNA，这一活性也与RecA蛋白有关。RecO蛋白促进的链同化反应需要Mg 2+，并且是ATP独立的。由于RecO和RecA蛋白之间的生物化学相似性，本研究还评估了RecO蛋白在体内DNA修复中替代RecA蛋白的能力。结果表明，RecO蛋白的过表达部分抑制了recA无效突变体的UV修复缺陷，并支持RecO和RecA蛋白在链同化和增强UV存活能力方面功能相似的假设。这些结果表明，RecO和RecA蛋白可能具有共同的功能特性。
The recO gene product is required for DNA repair and some types of homologous recombination in wild-type Escherichia coli cells. RecO protein has been previously purified and shown to bind to single- and double-stranded DNA and to promote the renaturation of complementary single-stranded DNA molecules. In this study, purified RecO protein was shown to catalyze the assimilation of single-stranded DNA into homologous superhelical double-stranded DNA, an activity also associated with RecA protein. The RecO protein-promoted strand assimilation reaction requires Mg2+ and is ATP independent. Because of the biochemical similarities between RecO and RecA proteins, the ability of RecO protein to substitute for RecA protein in DNA repair in vivo was also assessed in this study. The results show that overexpression of RecO protein partially suppressed the UV repair deficiency of a recA null mutant and support the hypothesis that RecO and RecA proteins are functionally similar with respect to strand assimilation and the ability to enhance UV survival. These results suggest that RecO and RecA proteins may have common functional properties.