A CHIMERIC REC-A PROTEIN THAT IMPLICATES NON-WATSON-CRICK INTERACTIONS IN HOMOLOGOUS PAIRING

被引：11

作者：

KURUMIZAKA, H

RAO, BJ

OGAWA, T

RADDING, CM

SHIBATA, T

机构：

[1] INST PHYS & CHEM RES,MOLEC & CELLULAR BIOL LAB,WAKO,SAITAMA 35101,JAPAN

[2] SAITAMA UNIV,GRAD SCH SCI & ENGN,URAWA,SAITAMA 338,JAPAN

[3] YALE UNIV,SCH MED,DEPT GENET & MOLEC BIOPHYS & BIOCHEM,NEW HAVEN,CT 06510

[4] OSAKA UNIV,FAC SCI,DEPT BIOL,TOYONAKA,OSAKA 560,JAPAN

来源：

NUCLEIC ACIDS RESEARCH | 1994年 / 22卷 / 16期

关键词：

D O I：

10.1093/nar/22.16.3387

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 helical filament formed by RecA protein on single-stranded DNA plays an important role in homologous recombination and pairs with a complementary single strand or homologous duplex DNA. The RecA nucleoprotein filament also recognizes an identical single strand. The chimeric protein, RecAc38, forms a nucleoprotein filament that recognizes a complementary strand but is defective in recognition of duplex DNA, and is associated with phenotypic defects in repair and recombination. As described here, RecAc38 nucleoprotein filament is also defective in recognition of an identical strand, either when the filament has within it a single strand or duplex DNA. A model that postulates three DNA binding sites rationalizes these observations and suggests that the third binding site mediates non-Watson-Crick interactions that are instrumental in recognition of homology in duplex DNA.

引用

页码：3387 / 3391

页数：5

共 22 条

[11]

RADDING CM, 1991, J BIOL CHEM, V266, P5355

[12] GENE STRUCTURE AND EXPRESSION - HELICAL RECA NUCLEOPROTEIN FILAMENTS MEDIATE HOMOLOGOUS PAIRING AND STRAND EXCHANGE [J].