The interaction of recombination proteins with supercoiled DNA: defining the role of supercoiling in lambda integrative recombination.

Abstract:

:Lambda integrative recombination depends on supercoiling of the phage attachment site, attP. Using dimethylsulfate protection and indirect end-labeling, the interaction of the recombination proteins Int and IHF with supercoiled and linear attP has been studied. Supercoiling enhances the binding of Int to attP, but not if a truncated attP site is employed or if IHF is omitted. We reason that the altered affinity reflects the formation of a higher-order nucleoprotein structure, an "attP intasome," that involves Int and IHF assembly of both arms of attP into a wrapped configuration. The good correlation between the degree and sign of supercoiling needed to promote recombination and that needed for the "attP intasome" indicates that the primary role of supercoiling is to drive the formation of the wrapped structure.

journal_name

Cell

journal_title

Cell

authors

Richet E,Abcarian P,Nash HA

doi

10.1016/0092-8674(86)90700-2

subject

Has Abstract

pub_date

1986-09-26 00:00:00

pages

1011-21

issue

7

eissn

0092-8674

issn

1097-4172

pii

0092-8674(86)90700-2

journal_volume

46

pub_type

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