Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-07

AUTHORS

U Grawunder, M Wilm, X Wu, P Kulesza, T E Wilson, M Mann, M R Lieber

ABSTRACT

Mutation of the XRCC4 gene in mammalian cells prevents the formation of the signal and coding joints in the V(D)J recombination reaction, which is necessary for production of a functional immunoglobulin gene, and renders the cells highly sensitive to ionizing radiation. However, XRCC4 shares no sequence homology with other proteins, nor does it have a biochemical activity to indicate what its function might be. Here we show that DNA ligase IV co-immunoprecipitates with XRCC4 and that these two proteins specifically interact with one another in a yeast two-hybrid system. Ligation of DNA double-strand breaks in a cell-free system by DNA ligase IV is increased fivefold by purified XRCC4 and seven- to eightfold when XRCC4 is co-expressed with DNA ligase IV. We conclude that the biological consequences of mutating XRCC4 are primarily due to the loss of its stimulatory effect on DNA ligase IV: the function of the XRCC4-DNA ligase IV complex may be to carry out the final steps of V(D)J recombination and joining of DNA ends. More... »

PAGES

492-495

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/41358

DOI

http://dx.doi.org/10.1038/41358

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1023520765

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9242410


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