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The HMGB1 acidic tail regulates HMGB1 DNA binding specificity by a unique mechanism.

Abstract：

:HMGB1 is a conserved chromosomal protein composed of two DNA-binding domains and an acidic C-terminal tail. There were evidences suggesting that the C-terminal tail contributed to the DNA binding specificity of the N-terminal DNA-binding domains. However, the mechanism underlining this observation is largely unknown. Our data first confirmed the previous study with NMR that showed a direct interaction between HMGB1's C-terminal tail and its N-terminal domains. We further demonstrated that this interaction can be competed more efficiently by a DNA with four-way junction structure than by a linear double-stranded DNA. Mutations within the N-terminal region, that disrupt its binding to the C-terminal tail, abolished HMGB1's ability to distinguish the linear DNA and the four-way junction DNA. Those data suggested a unique mechanism designed by nature that utilizes a protein's negatively charged C-terminal tail to enhance its DNA-binding domain's specificity to certain structured DNAs.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Wang Q,Zeng M,Wang W,Tang J

doi

10.1016/j.bbrc.2007.05.130

subject

Has Abstract

pub_date

2007-08-17 00:00:00

pages

14-9

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(07)01124-2

journal_volume

360

pub_type

杂志文章

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