RGD Reference Report - Characterization of the redox transition of the XRCC1 N-terminal domain. - Rat Genome Database

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Characterization of the redox transition of the XRCC1 N-terminal domain.

Authors: Gabel, Scott A  Smith, Cassandra E  Cuneo, Matthew J  Mueller, Geoffrey A  Kirby, Thomas W  DeRose, Eugene F  Krahn, Juno M  London, Robert E 
Citation: Gabel SA, etal., Structure. 2014 Dec 2;22(12):1754-63. doi: 10.1016/j.str.2014.09.012. Epub 2014 Nov 13.
RGD ID: 13432291
Pubmed: PMID:25456813   (View Abstract at PubMed)
PMCID: PMC5588702   (View Article at PubMed Central)
DOI: DOI:10.1016/j.str.2014.09.012   (Journal Full-text)

XRCC1, a scaffold protein involved in DNA repair, contains an N-terminal domain (X1NTD) that interacts specifically with DNA polymerase ß. It was recently discovered that X1NTD contains a disulfide switch that allows it to adopt either of two metamorphic structures. In the present study, we demonstrate that formation of an N-terminal proline carbimate adduct resulting from the nonenzymatic reaction of Pro2 with CO2 is essential for stabilizing the oxidized structure, X1NTDox. The kinetic response of X1NTDred to H2O2, monitored by NMR, was determined to be very slow, consistent with involvement of the buried, kinetically trapped Cys12 residue, but was significantly accelerated by addition of protein disulfide isomerase or by Cu(2+). NMR analysis of a sample containing the pol ß polymerase domain, and both the reduced and oxidized forms of X1NTD, indicates that the oxidized form binds to the enzyme 25-fold more tightly than the reduced form.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein binding enablesIPIUniProtKB:P1888713432291PMID:25456813IntAct 

Objects Annotated

Genes (Rattus norvegicus)
Polb  (DNA polymerase beta)


Additional Information