DsRed-mediated oligomerization stabilizes HMGB1 on chromatin in vivo and on DNA in vitro

被引：2

作者：

Messmer, Melanie ^{[1
]}

Klein, Christophe ^{[1
]}

Boniface, Rachel ^{[1
]}

Gnaedig, Nina F. ^{[1
]}

Lecerf, Maxime ^{[1
]}

Barnay-Verdier, Stephanie ^{[1
]}

Marechal, Vincent ^{[1
]}

机构：

[1] Univ Paris 05, Ctr Rech Cordeliers, Univ Paris 06, INSERM,UMRS 872, F-75006 Nice, France

来源：

BIOCHIMIE | 2013年 / 95卷 / 04期

关键词：

HMGB1; mobility; DsRed-mediated oligomerization; Chromatin; FRAP; CISPLATIN-MODIFIED DNA; TRANSCRIPTION FACTOR; PROTEINS; RECOGNITION; BINDING; DOMAIN; EXPRESSION; XUBF;

D O I：

10.1016/j.biochi.2012.11.001

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

High-mobility group box-1 (HMGB1) is remarkably mobile in living cells, which reflects its ability to interact only transiently with both DNA and protein. This property is likely essential for HMGB1 nuclear activities. Nonetheless the weak interaction of HMGB1 with DNA and/or protein partners has also been a major limitation for investigating HMGB1 subnuclear localisation and for the identification of HMGB1 containing complexes by conventional biochemical approaches. In the present study, FRAP experiments demonstrated that DsRed-mediated oligomerization strongly reduces HMGB1 mobility due to an increased affinity for cellular chromatin. Moreover, oligomerized DsRed HMGB1 exhibited a higher affinity for supercoiled DNA in vitro compared to its monomeric counterpart. These results indicate that DsRed-meditated oligomerization is prone to stabilize labile interactions involving HMGB1 both in vivo and in vitro. (C) 2012 Elsevier Masson SAS. All rights reserved.

引用

页码：962 / 966

页数：5

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