A chimeric Rec-A protein that implicates non-Watson - Crick interactions in homologous pairing

Hitoshi Kurumizaka; B. J. Rao; Tomoko Ogawa; Charles M. Radding; Takehiko Shibata

A chimeric Rec-A protein that implicates non-Watson - Crick interactions in homologous pairing

Hitoshi Kurumizaka, B. J. Rao, Tomoko Ogawa, Charles M. Radding, Takehiko Shibata^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	3387-3391
Number of pages	5
Journal	Nucleic Acids Research
Volume	22
Issue number	16
Publication status	Published - 1994 Aug 25
Externally published	Yes

ASJC Scopus subject areas

Genetics
Statistics, Probability and Uncertainty
Applied Mathematics
Health, Toxicology and Mutagenesis
Toxicology
Genetics(clinical)

Cite this

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title = "A chimeric Rec-A protein that implicates non-Watson - Crick interactions in homologous pairing",

abstract = "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.",

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T1 - A chimeric Rec-A protein that implicates non-Watson - Crick interactions in homologous pairing

AU - Kurumizaka, Hitoshi

AU - Rao, B. J.

AU - Ogawa, Tomoko

AU - Radding, Charles M.

AU - Shibata, Takehiko

PY - 1994/8/25

Y1 - 1994/8/25

N2 - 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.

AB - 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.

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A chimeric Rec-A protein that implicates non-Watson - Crick interactions in homologous pairing

Abstract

ASJC Scopus subject areas

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