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Transient HMGB protein interactions with B-DNA duplexes and complexes.

Abstract：

:HMGB proteins are abundant, non-histone proteins in eukaryotic chromatin. HMGB proteins contain one or two conserved "HMG boxes" and can be sequence-specific or nonspecific in their DNA binding. HMGB proteins cause strong DNA bending and bind preferentially to deformed DNAs. We wish to understand how HMGB proteins increase the apparent flexibility of non-distorted B-form DNA. We test the hypothesis that HMGB proteins bind transiently, creating an ensemble of distorted DNAs with rapidly interconverting conformations. We show that binding of B-form DNA by HMGB proteins is both weak and transient under conditions where DNA cyclization is strongly enhanced. We also detect novel complexes in which HMGB proteins simultaneously bind more than one DNA duplex.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Zimmerman J,Maher LJ 3rd

doi

10.1016/j.bbrc.2008.04.024

subject

Has Abstract

pub_date

2008-06-20 00:00:00

pages

79-84

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)00650-5

journal_volume

371

pub_type

杂志文章

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