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The double life of HMGB1 chromatin protein: architectural factor and extracellular signal.

Authors :
Müller, Susanne
Scaffidi, Paola
Degryse, Bernard
Bonaldi, Tiziana
Ronfani, Lorenza
Agresti, Alessandra
Beltrame, Monica
Bianchi, Marco E.
Source :
EMBO Journal; 8/15/2001, Vol. 20 Issue 16, p4337-4340, 4p
Publication Year :
2001

Abstract

This article focuses on the high mobility group box (HMGB) chromosomal proteins. The HMGB family comprises the three proteins HMGB1, HMGB2 and HMBG3. The structure of these three proteins is highly conserved, and their biochemical properties are so far indistinguishable. HMGBs are composed of three different domains. The localization of these proteins in most cells is nuclear. In their nuclear identity, HMGB1 and HMGB2 bind to the minor groove of DNA, causing a local distortion of the double helix. They have little or no sequence preference and they are recruited to the site of action by specific DNA binding proteins.

Details

Language :
English
ISSN :
02614189
Volume :
20
Issue :
16
Database :
Complementary Index
Journal :
EMBO Journal
Publication Type :
Academic Journal
Accession number :
12955298
Full Text :
https://doi.org/10.1093/emboj/20.16.4337