RECA-CENTER-DOT-OLIGONUCLEOTIDE FILAMENTS BIND IN THE MINOR-GROOVE OF DOUBLE-STRANDED DNA

被引：48

作者：

BALIGA, R ^{[1
]}

SINGLETON, JW ^{[1
]}

DERVAN, PB ^{[1
]}

机构：

[1] CALTECH, DIV CHEM & CHEM ENGN, PASADENA, CA 91125 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 22期

关键词：

D O I：

10.1073/pnas.92.22.10393

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Escherichia coli RecA protein, in the presence of ATP or its analog adenosine 5'-[gamma-thio]triphosphate, polymerizes on single-stranded DNA to form nucleoprotein filaments that can then bind to homologous sequences on duplex DNA. The three-stranded joint molecule formed as a result of this binding event is a key intermediate in general recombination. We have used affinity cleavage to examine this three-stranded joint by incorporating a single thymidine-EDTA . Fe (T*) into the oligonucleotide part of the filament. Our analysis of the cleavage patterns from the joint molecule reveals that the nncleoprotein filament binds in the mirror groove of an extended Watson-Crick duplex.

引用

页码：10393 / 10397

页数：5

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