Specific defects in double-stranded DNA unwinding and homologous pairing of a mutant RecA protein

Hitoshi Kurumizaka; Hideki Aihara; Shukuko Ikawa; Takehiko Shibata

doi:10.1016/S0014-5793(00)01781-6

Specific defects in double-stranded DNA unwinding and homologous pairing of a mutant RecA protein

Hitoshi Kurumizaka^*, Hideki Aihara, Shukuko Ikawa, Takehiko Shibata

^*Corresponding author for this work

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

4 Citations (Scopus)

Abstract

The DNA molecules bound to RecA filaments are extended 1.5-fold relative to B-form DNA. This extended DNA structure may be important in the recognition of homology between single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). In this study, we show that the K286N mutation specifically impaired the dsDNA unwinding and homologous pairing activities of RecA, without an apparent effect on dsDNA binding itself. In contrast, the R243Q mutation caused defective dsDNA unwinding, due to the defective dsDNA binding of the C-terminal domain of RecA. These results provide new evidence that dsDNA unwinding is essential to homology recognition between ssDNA and dsDNA during homologous pairing. Copyright (C) 2000 Federation of European Biochemical Societies.

Original language	English
Pages (from-to)	129-134
Number of pages	6
Journal	FEBS Letters
Volume	477
Issue number	1-2
DOIs	https://doi.org/10.1016/S0014-5793(00)01781-6
Publication status	Published - 2000 Jul 14
Externally published	Yes

Keywords

DNA binding
DNA unwinding
Homologous pairing
RecA
RecA mutant
Recombination

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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10.1016/S0014-5793(00)01781-6

Cite this

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title = "Specific defects in double-stranded DNA unwinding and homologous pairing of a mutant RecA protein",

abstract = "The DNA molecules bound to RecA filaments are extended 1.5-fold relative to B-form DNA. This extended DNA structure may be important in the recognition of homology between single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). In this study, we show that the K286N mutation specifically impaired the dsDNA unwinding and homologous pairing activities of RecA, without an apparent effect on dsDNA binding itself. In contrast, the R243Q mutation caused defective dsDNA unwinding, due to the defective dsDNA binding of the C-terminal domain of RecA. These results provide new evidence that dsDNA unwinding is essential to homology recognition between ssDNA and dsDNA during homologous pairing. Copyright (C) 2000 Federation of European Biochemical Societies.",

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T1 - Specific defects in double-stranded DNA unwinding and homologous pairing of a mutant RecA protein

AU - Kurumizaka, Hitoshi

AU - Aihara, Hideki

AU - Ikawa, Shukuko

AU - Shibata, Takehiko

PY - 2000/7/14

Y1 - 2000/7/14

N2 - The DNA molecules bound to RecA filaments are extended 1.5-fold relative to B-form DNA. This extended DNA structure may be important in the recognition of homology between single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). In this study, we show that the K286N mutation specifically impaired the dsDNA unwinding and homologous pairing activities of RecA, without an apparent effect on dsDNA binding itself. In contrast, the R243Q mutation caused defective dsDNA unwinding, due to the defective dsDNA binding of the C-terminal domain of RecA. These results provide new evidence that dsDNA unwinding is essential to homology recognition between ssDNA and dsDNA during homologous pairing. Copyright (C) 2000 Federation of European Biochemical Societies.

AB - The DNA molecules bound to RecA filaments are extended 1.5-fold relative to B-form DNA. This extended DNA structure may be important in the recognition of homology between single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). In this study, we show that the K286N mutation specifically impaired the dsDNA unwinding and homologous pairing activities of RecA, without an apparent effect on dsDNA binding itself. In contrast, the R243Q mutation caused defective dsDNA unwinding, due to the defective dsDNA binding of the C-terminal domain of RecA. These results provide new evidence that dsDNA unwinding is essential to homology recognition between ssDNA and dsDNA during homologous pairing. Copyright (C) 2000 Federation of European Biochemical Societies.

KW - DNA binding

KW - DNA unwinding

KW - Homologous pairing

KW - RecA

KW - RecA mutant

KW - Recombination

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Specific defects in double-stranded DNA unwinding and homologous pairing of a mutant RecA protein

Abstract

Keywords

ASJC Scopus subject areas

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