Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA

Stefan Sigurdsson, Kelly Trujillo, Bin Wei Song, Sabrina Stratton, Patrick Sung

Research output: Contribution to journalArticle

126 Citations (Scopus)

Abstract

Human Rad51 (hRad51), a member of a conserved family of general recombinases, is shown here to have an avid capability to make DNA joints between homologous DNA molecules and promote highly efficient DNA strand exchange of the paired molecules over at least 5.4 kilobase pairs. Furthermore, maximal efficiency of homologous DNA pairing and strand exchange is strongly dependent on the heterotrimeric single-stranded DNA binding factor hRPA and requires conditions that lessen interactions of the homologous duplex with the hRad51-single-stranded DNA nucleoprotein filament. The homologous DNA pairing and strand exchange system described should be valuable for dissecting the action mechanism of hRad51 and for deciphering its functional interactions with other recombination factors.

Original languageEnglish (US)
Pages (from-to)8798-8806
Number of pages9
JournalJournal of Biological Chemistry
Volume276
Issue number12
DOIs
StatePublished - Mar 23 2001

Fingerprint

DNA
Single-Stranded DNA
Recombinases
Molecules
Nucleoproteins
Genetic Recombination
Joints

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Sigurdsson, S., Trujillo, K., Song, B. W., Stratton, S., & Sung, P. (2001). Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA. Journal of Biological Chemistry, 276(12), 8798-8806. https://doi.org/10.1074/jbc.M010011200

Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA. / Sigurdsson, Stefan; Trujillo, Kelly; Song, Bin Wei; Stratton, Sabrina; Sung, Patrick.

In: Journal of Biological Chemistry, Vol. 276, No. 12, 23.03.2001, p. 8798-8806.

Research output: Contribution to journalArticle

Sigurdsson, S, Trujillo, K, Song, BW, Stratton, S & Sung, P 2001, 'Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA', Journal of Biological Chemistry, vol. 276, no. 12, pp. 8798-8806. https://doi.org/10.1074/jbc.M010011200
Sigurdsson, Stefan ; Trujillo, Kelly ; Song, Bin Wei ; Stratton, Sabrina ; Sung, Patrick. / Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 12. pp. 8798-8806.
@article{218e8303be59494daba7236913bc8811,
title = "Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA",
abstract = "Human Rad51 (hRad51), a member of a conserved family of general recombinases, is shown here to have an avid capability to make DNA joints between homologous DNA molecules and promote highly efficient DNA strand exchange of the paired molecules over at least 5.4 kilobase pairs. Furthermore, maximal efficiency of homologous DNA pairing and strand exchange is strongly dependent on the heterotrimeric single-stranded DNA binding factor hRPA and requires conditions that lessen interactions of the homologous duplex with the hRad51-single-stranded DNA nucleoprotein filament. The homologous DNA pairing and strand exchange system described should be valuable for dissecting the action mechanism of hRad51 and for deciphering its functional interactions with other recombination factors.",
author = "Stefan Sigurdsson and Kelly Trujillo and Song, {Bin Wei} and Sabrina Stratton and Patrick Sung",
year = "2001",
month = "3",
day = "23",
doi = "10.1074/jbc.M010011200",
language = "English (US)",
volume = "276",
pages = "8798--8806",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "12",

}

TY - JOUR

T1 - Basis for Avid Homologous DNA Strand Exchange by Human Rad51 and RPA

AU - Sigurdsson, Stefan

AU - Trujillo, Kelly

AU - Song, Bin Wei

AU - Stratton, Sabrina

AU - Sung, Patrick

PY - 2001/3/23

Y1 - 2001/3/23

N2 - Human Rad51 (hRad51), a member of a conserved family of general recombinases, is shown here to have an avid capability to make DNA joints between homologous DNA molecules and promote highly efficient DNA strand exchange of the paired molecules over at least 5.4 kilobase pairs. Furthermore, maximal efficiency of homologous DNA pairing and strand exchange is strongly dependent on the heterotrimeric single-stranded DNA binding factor hRPA and requires conditions that lessen interactions of the homologous duplex with the hRad51-single-stranded DNA nucleoprotein filament. The homologous DNA pairing and strand exchange system described should be valuable for dissecting the action mechanism of hRad51 and for deciphering its functional interactions with other recombination factors.

AB - Human Rad51 (hRad51), a member of a conserved family of general recombinases, is shown here to have an avid capability to make DNA joints between homologous DNA molecules and promote highly efficient DNA strand exchange of the paired molecules over at least 5.4 kilobase pairs. Furthermore, maximal efficiency of homologous DNA pairing and strand exchange is strongly dependent on the heterotrimeric single-stranded DNA binding factor hRPA and requires conditions that lessen interactions of the homologous duplex with the hRad51-single-stranded DNA nucleoprotein filament. The homologous DNA pairing and strand exchange system described should be valuable for dissecting the action mechanism of hRad51 and for deciphering its functional interactions with other recombination factors.

UR - http://www.scopus.com/inward/record.url?scp=0035937811&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035937811&partnerID=8YFLogxK

U2 - 10.1074/jbc.M010011200

DO - 10.1074/jbc.M010011200

M3 - Article

C2 - 11124265

AN - SCOPUS:0035937811

VL - 276

SP - 8798

EP - 8806

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 12

ER -