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High mobility group nucleosomal binding domain 2 (HMGN2) sumoylation by the SUMO E3 ligase PIAS1 decreases the binding affinity to nucleosome core particles

Authors
 Jie Wu  ;  Sol Kim  ;  Man Sup Kwak  ;  Jang Bin Jeong  ;  Hyun Jin Min  ;  Ho-Geun Yoon  ;  Jin-Hyun Ahn  ;  Jeon-Soo Shin 
Citation
 JOURNAL OF BIOLOGICAL CHEMISTRY, Vol.289(29) : 20000-20011, 2014 
Journal Title
 JOURNAL OF BIOLOGICAL CHEMISTRY 
ISSN
 0021-9258 
Issue Date
2014
MeSH
Amino Acid Sequence ; Amino Acid Substitution ; Binding Sites/genetics ; Cell Line ; Cysteine Endopeptidases ; Endopeptidases/genetics ; Endopeptidases/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; HEK293 Cells ; HMGN2 Protein/chemistry ; HMGN2 Protein/genetics ; HMGN2 Protein/metabolism* ; HeLa Cells ; Humans ; Lysine/chemistry ; Molecular Sequence Data ; Nucleosomes/metabolism* ; Protein Binding ; Protein Inhibitors of Activated STAT/genetics ; Protein Inhibitors of Activated STAT/metabolism* ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; SUMO-1 Protein/genetics ; SUMO-1 Protein/metabolism ; Sequence Homology, Amino Acid ; Small Ubiquitin-Related Modifier Proteins/genetics ; Small Ubiquitin-Related Modifier Proteins/metabolism* ; Sumoylation ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism*
Keywords
Chromatin Regulation ; HMGN2 ; Inflammation ; Molecular Cell Biology ; Nucleosome ; Sumoylation
Abstract
High mobility group nucleosomal binding domain 2 (HMGN2) is a small and unique non-histone protein that has many functions in a variety of cellular processes, including regulation of chromatin structure, transcription, and DNA repair. In addition, it may have other roles in antimicrobial activity, cell homing, and regulating cytokine release. Although the biochemical properties of HMGN2 protein are regulated by acetylation and phosphorylation, it is not yet known whether HMGN2 activity can also be regulated by SUMOylation. In this study, we demonstrated for the first time that HMGN2 is modified by covalent attachment of small ubiquitin-related modifier 1 (SUMO1) by pro-inflammatory signal and identified the major SUMOylated lysine residues that localize to the HMGN2 nucleosome-binding domain at Lys-17 and Lys-35. SENP1 can deSUMOylate SUMOylated HMGN2, and PIAS1 is the E3 ligase responsible for SUMOylation of HMGN2. Finally, using SUMO1-conjugated HMGN2 purified from a basal SUMOylation system in Escherichia coli, we demonstrated that SUMOylated HMGN2 has decreased the binding affinity to nucleosome core particles in comparison to unSUMOylated HMGN2. These observations potentially provide new perspectives for understanding the functions of HMGN2 in inflammatory reaction.
Full Text
http://www.jbc.org/content/289/29/20000.long
DOI
10.1074/jbc.M114.555425
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Biochemistry and Molecular Biology (생화학-분자생물학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Otorhinolaryngology (이비인후과학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
Yonsei Authors
Kwak, Man Sup(곽만섭) ORCID logo https://orcid.org/0000-0002-3989-3016
Min, Hyun Jin(민현진)
Shin, Jeon Soo(신전수) ORCID logo https://orcid.org/0000-0002-8294-3234
Yoon, Ho Geun(윤호근) ORCID logo https://orcid.org/0000-0003-2718-3372
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/99242
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