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The structure of Xis reveals the basis for filament formation and insight into DNA bending within a mycobacteriophage intasome.

Abstract：

:The recombination directionality factor, Xis, is a DNA bending protein that determines the outcome of integrase-mediated site-specific recombination by redesign of higher-order protein-DNA architectures. Although the attachment site DNA of mycobacteriophage Pukovnik is likely to contain four sites for Xis binding, Xis crystals contain five subunits in the asymmetric unit, four of which align into a Xis filament and a fifth that is generated by an unusual domain swap. Extensive intersubunit contacts stabilize a bent filament-like arrangement with Xis monomers aligned head to tail. The structure implies a DNA bend of ~120°, which is in agreement with DNA bending measured in vitro. Formation of attR-containing intasomes requires only Int and Xis, distinguishing Pukovnik from lambda. Therefore, we conclude that, in Pukovnik, Xis-induced DNA bending is sufficient to promote intramolecular Int-mediated bridges during intasome formation.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Singh S,Plaks JG,Homa NJ,Amrich CG,Héroux A,Hatfull GF,VanDemark AP

doi

10.1016/j.jmb.2013.10.002

subject

Has Abstract

pub_date

2014-01-23 00:00:00

pages

412-22

issue

2

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(13)00628-1

journal_volume

426

pub_type

杂志文章

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