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PMID: 20123074 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Review

HMGB1: roles in base excision repair and related function.

Biochimica et biophysica acta ·Vol. 1799 ·No. 1-2 ·2010-00-00 ·Pages 119-30

Liu Y, Prasad R, Wilson SH

Abstract

High mobility group box 1 (HMGB1) is a nonhistone architectural protein that is involved in many biological processes including chromatin remodeling, transcription, cell signaling of inflammation, DNA damage repair and others. Recent studies have identified the cross-link of HMGB1 with a DNA base excision repair intermediate indicating that this protein is involved in base excision repair (BER) pathway. Further characterization of the roles of HMGB1 in BER demonstrates that the protein acts as a cofactor to regulate BER sub-pathways by inhibiting single-nucleotide BER and stimulating long-patch BER through modulating the activities of base excision repair enzymes. Directing of base lesion repair to the long-patch sub-pathway can result in trinucleotide repeat instability suggesting an important role of HMGB1 in modulating genome stability.

MeSH Terms
Animals DNA Breaks, Single-Stranded DNA Repair Genomic Instability HMGB1 Protein/metabolism Humans Models, Biological Trinucleotide Repeat Expansion/genetics
Chemicals
HMGB1 Protein
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Liu Yuan
Laboratory of Structural Biology, The National Institute of Environmental Health Sciences, National Institutes of Health, 111 T. W. Alexander Drive Research Triangle Park, NC 27709, USA.
Prasad Rajendra
Wilson Samuel H
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Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
2010-00-00
Pages
119-30
Language
English
Region
Netherlands
NLM ID
0217513
PMCID
PMC2818529
Subset
IM
Grants
Intramural NIH HHS · Z01 ES050158-11 · United States
Intramural NIH HHS · Z01 ES050159 · United States
Intramural NIH HHS · Z01 ES050159-11 · United States
NIEHS NIH HHS · Z01-ES010158 · United States
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