Twisting and untwisting a single DNA molecule covered by RecA protein.

Abstract:

:We study dsDNA-RecA interactions by exerting forces in the pN range on single DNA molecules while the interstrand topological state is controlled owing to a magnetic tweezers setup. We show that unwinding a duplex DNA molecule induces RecA polymerization even at moderate force. Once initial polymerization has nucleated, the extent of RecA coverage still depends on the degree of supercoiling: exerting a positive or negative torsional constraint on the fiber forces partial depolymerization, with a strikingly greater stability when ATPgammaS is used as a cofactor instead of ATP. This nucleofilament's sensitivity to topology might be a way for the bacterial cell to limit consumption of precious RecA monomers when DNA damage is addressed through homologous recombination repair.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Fulconis R,Bancaud A,Allemand JF,Croquette V,Dutreix M,Viovy JL

doi

10.1529/biophysj.104.043059

subject

Has Abstract

pub_date

2004-10-01 00:00:00

pages

2552-63

issue

4

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(04)73726-1

journal_volume

87

pub_type

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