Role of interaction between two silkworm RecA homologs in homologous DNA pairing

Takahiro Kusakabe, Yutaka Kawaguchi, Takuji Maeda, Katsumi Koga

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Recombinant BmRad51 and BmDmc1, silkworm homologs of the Escherichia coli RecA proteins catalyzing the homologous DNA pairing, were purified from E. coli cells carrying expression vectors. These possessed different enzymatic properties in the joint molecule formation between single-stranded circular DNA and homologous linear double-stranded DNA. The requirement of single-stranded circular DNA for the efficient reaction was twofold higher in BmRad51 than in BmDmc1. Although able to mediate the joint molecule formation independently, a complex of the two enzymes formed prior to single-stranded DNA binding was found to have augmented efficiency of the pairing reaction.

Original languageEnglish
Pages (from-to)39-44
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume388
Issue number1
DOIs
Publication statusPublished - Apr 1 2001

Fingerprint

Circular DNA
Bombyx
Single-Stranded DNA
Escherichia coli
Rec A Recombinases
Molecules
DNA
Joints
Escherichia coli Proteins
Enzymes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Role of interaction between two silkworm RecA homologs in homologous DNA pairing. / Kusakabe, Takahiro; Kawaguchi, Yutaka; Maeda, Takuji; Koga, Katsumi.

In: Archives of Biochemistry and Biophysics, Vol. 388, No. 1, 01.04.2001, p. 39-44.

Research output: Contribution to journalArticle

Kusakabe, Takahiro ; Kawaguchi, Yutaka ; Maeda, Takuji ; Koga, Katsumi. / Role of interaction between two silkworm RecA homologs in homologous DNA pairing. In: Archives of Biochemistry and Biophysics. 2001 ; Vol. 388, No. 1. pp. 39-44.
@article{c5031464e0a641f2ac667d8e9439838a,
title = "Role of interaction between two silkworm RecA homologs in homologous DNA pairing",
abstract = "Recombinant BmRad51 and BmDmc1, silkworm homologs of the Escherichia coli RecA proteins catalyzing the homologous DNA pairing, were purified from E. coli cells carrying expression vectors. These possessed different enzymatic properties in the joint molecule formation between single-stranded circular DNA and homologous linear double-stranded DNA. The requirement of single-stranded circular DNA for the efficient reaction was twofold higher in BmRad51 than in BmDmc1. Although able to mediate the joint molecule formation independently, a complex of the two enzymes formed prior to single-stranded DNA binding was found to have augmented efficiency of the pairing reaction.",
author = "Takahiro Kusakabe and Yutaka Kawaguchi and Takuji Maeda and Katsumi Koga",
year = "2001",
month = "4",
day = "1",
doi = "10.1006/abbi.2001.2275",
language = "English",
volume = "388",
pages = "39--44",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Role of interaction between two silkworm RecA homologs in homologous DNA pairing

AU - Kusakabe, Takahiro

AU - Kawaguchi, Yutaka

AU - Maeda, Takuji

AU - Koga, Katsumi

PY - 2001/4/1

Y1 - 2001/4/1

N2 - Recombinant BmRad51 and BmDmc1, silkworm homologs of the Escherichia coli RecA proteins catalyzing the homologous DNA pairing, were purified from E. coli cells carrying expression vectors. These possessed different enzymatic properties in the joint molecule formation between single-stranded circular DNA and homologous linear double-stranded DNA. The requirement of single-stranded circular DNA for the efficient reaction was twofold higher in BmRad51 than in BmDmc1. Although able to mediate the joint molecule formation independently, a complex of the two enzymes formed prior to single-stranded DNA binding was found to have augmented efficiency of the pairing reaction.

AB - Recombinant BmRad51 and BmDmc1, silkworm homologs of the Escherichia coli RecA proteins catalyzing the homologous DNA pairing, were purified from E. coli cells carrying expression vectors. These possessed different enzymatic properties in the joint molecule formation between single-stranded circular DNA and homologous linear double-stranded DNA. The requirement of single-stranded circular DNA for the efficient reaction was twofold higher in BmRad51 than in BmDmc1. Although able to mediate the joint molecule formation independently, a complex of the two enzymes formed prior to single-stranded DNA binding was found to have augmented efficiency of the pairing reaction.

UR - http://www.scopus.com/inward/record.url?scp=0035298440&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035298440&partnerID=8YFLogxK

U2 - 10.1006/abbi.2001.2275

DO - 10.1006/abbi.2001.2275

M3 - Article

VL - 388

SP - 39

EP - 44

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -