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

B. Franklin Pugh; Brian C. Schutte; Michael M. Cox

doi:10.1016/0022-2836(89)90219-2

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

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

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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 language	English (US)
Pages (from-to)	487-492
Number of pages	6
Journal	Journal of Molecular Biology
Volume	205
Issue number	3
DOIs	https://doi.org/10.1016/0022-2836(89)90219-2
State	Published - Feb 5 1989

All Science Journal Classification (ASJC) codes

Structural Biology
Molecular Biology

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10.1016/0022-2836(89)90219-2

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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, {B. Franklin} and Schutte, {Brian C.} and Cox, {Michael M.}",

note = "Funding Information: by NIH grant GM32335 NIH Research Career",

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

AU - Pugh, B. Franklin

AU - Schutte, Brian C.

AU - Cox, Michael M.

N1 - Funding Information: by NIH grant GM32335 NIH Research Career

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.

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

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