RGD Reference Report - Non-histone chromosomal proteins HMG1 and 2 enhance ligation reaction of DNA double-strand breaks. - Rat Genome Database

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Non-histone chromosomal proteins HMG1 and 2 enhance ligation reaction of DNA double-strand breaks.

Authors: Nagaki, S  Yamamoto, M  Yumoto, Y  Shirakawa, H  Yoshida, M  Teraoka, H 
Citation: Nagaki S, etal., Biochem Biophys Res Commun. 1998 May 8;246(1):137-41.
RGD ID: 1601271
Pubmed: PMID:9600082   (View Abstract at PubMed)
DOI: DOI:10.1006/bbrc.1998.8589   (Journal Full-text)

DNA ligase IV in a complex with XRCC4 is responsible for DNA end-joining in repair of DNA double-strand breaks (DSB) and V(D)J recombination. We found that non-histone chromosomal high mobility group (HMG) proteins 1 and 2 enhanced the ligation of linearized pUC119 DNA with DNA ligase IV from rat liver nuclear extract. Intra-molecular and inter-molecular ligations of cohesive-ended and blunt-ended DNA were markedly stimulated by HMG1 and 2. Recombinant HMG2-domain A, B, and (A + B) polypeptides were similarly, but non-identically, effective for the stimulation of DSB ligation reaction. Ligation of single-strand breaks (nicks) was only slightly activated by the HMG proteins. The DNA end-binding Ku protein singly or in combination with the catalytic component of DNA-dependent protein kinase (DNA-PK) as the DNA-PK holoenzyme was ineffective for the ligation of linearized pUC119 DNA. Although the stimulatory effect of HMG1 and 2 on ligation of DSB in vitro was not specific to DNA ligase IV, these results suggest that HMG1 and 2 are involved in the final ligation step in DNA end-joining processes of DSB repair and V(D)J recombination.



Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Lig4RatAMP binding  IDA  RGD 
Lig4RatDNA ligase (ATP) activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Lig4  (DNA ligase 4)


Additional Information