Extent of duplex DNA underwinding induced by RecA protein binding in the presence of ATP

Benjamin Franklin Pugh, Brian C. Schutte, Michael M. Cox

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

A method is described for the accurate determination of the superhelical density (σ) of highly underwound circular DNA molecules. Using this method, duplex DNA bound by RecA protein in the presence of ATP at pH 7.5 is found to be underwound by 39.6% (σ = -0.396), corresponding to a helical periodicity of 17.4 base-pairs per turn. The underwinding is increased to 41% (17.9 base-pairs per turn) in the presence of low levels of ATPγS, in good agreement with the 18.6 base-pairs per turn reported previously. In spite of the extensive underwinding, the distribution of DNA topoisomers produced by RecA protein binding is small. This indicates a high degree of structural uniformity among RecA-double-stranded DNA complexes in the presence of ATP.

Original languageEnglish (US)
Pages (from-to)487-492
Number of pages6
JournalJournal of Molecular Biology
Volume205
Issue number3
DOIs
StatePublished - Feb 5 1989

Fingerprint

Rec A Recombinases
Protein Binding
Base Pairing
Adenosine Triphosphate
DNA
Circular DNA
Periodicity

All Science Journal Classification (ASJC) codes

  • Virology

Cite this

@article{fc5b5257e890409e8bf42e62468e0cfd,
title = "Extent of duplex DNA underwinding induced by RecA protein binding in the presence of ATP",
abstract = "A method is described for the accurate determination of the superhelical density (σ) of highly underwound circular DNA molecules. Using this method, duplex DNA bound by RecA protein in the presence of ATP at pH 7.5 is found to be underwound by 39.6{\%} (σ = -0.396), corresponding to a helical periodicity of 17.4 base-pairs per turn. The underwinding is increased to 41{\%} (17.9 base-pairs per turn) in the presence of low levels of ATPγS, in good agreement with the 18.6 base-pairs per turn reported previously. In spite of the extensive underwinding, the distribution of DNA topoisomers produced by RecA protein binding is small. This indicates a high degree of structural uniformity among RecA-double-stranded DNA complexes in the presence of ATP.",
author = "Pugh, {Benjamin Franklin} and Schutte, {Brian C.} and Cox, {Michael M.}",
year = "1989",
month = "2",
day = "5",
doi = "10.1016/0022-2836(89)90219-2",
language = "English (US)",
volume = "205",
pages = "487--492",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "3",

}

Extent of duplex DNA underwinding induced by RecA protein binding in the presence of ATP. / Pugh, Benjamin Franklin; Schutte, Brian C.; Cox, Michael M.

In: Journal of Molecular Biology, Vol. 205, No. 3, 05.02.1989, p. 487-492.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Extent of duplex DNA underwinding induced by RecA protein binding in the presence of ATP

AU - Pugh, Benjamin Franklin

AU - Schutte, Brian C.

AU - Cox, Michael M.

PY - 1989/2/5

Y1 - 1989/2/5

N2 - A method is described for the accurate determination of the superhelical density (σ) of highly underwound circular DNA molecules. Using this method, duplex DNA bound by RecA protein in the presence of ATP at pH 7.5 is found to be underwound by 39.6% (σ = -0.396), corresponding to a helical periodicity of 17.4 base-pairs per turn. The underwinding is increased to 41% (17.9 base-pairs per turn) in the presence of low levels of ATPγS, in good agreement with the 18.6 base-pairs per turn reported previously. In spite of the extensive underwinding, the distribution of DNA topoisomers produced by RecA protein binding is small. This indicates a high degree of structural uniformity among RecA-double-stranded DNA complexes in the presence of ATP.

AB - A method is described for the accurate determination of the superhelical density (σ) of highly underwound circular DNA molecules. Using this method, duplex DNA bound by RecA protein in the presence of ATP at pH 7.5 is found to be underwound by 39.6% (σ = -0.396), corresponding to a helical periodicity of 17.4 base-pairs per turn. The underwinding is increased to 41% (17.9 base-pairs per turn) in the presence of low levels of ATPγS, in good agreement with the 18.6 base-pairs per turn reported previously. In spite of the extensive underwinding, the distribution of DNA topoisomers produced by RecA protein binding is small. This indicates a high degree of structural uniformity among RecA-double-stranded DNA complexes in the presence of ATP.

UR - http://www.scopus.com/inward/record.url?scp=0024511687&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024511687&partnerID=8YFLogxK

U2 - 10.1016/0022-2836(89)90219-2

DO - 10.1016/0022-2836(89)90219-2

M3 - Article

VL - 205

SP - 487

EP - 492

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 3

ER -