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PMID:9242410

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Citation

Grawunder, U, Wilm, M, Wu, X, Kulesza, P, Wilson, TE, Mann, M and Lieber, MR (1997) Activity of DNA ligase IV stimulated by complex formation with XRCC4 protein in mammalian cells. Nature 388:492-5

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.

Links

PubMed Online version:10.1038/41358

Keywords

Animals; CHO Cells; Cloning, Molecular; Cricetinae; DNA/metabolism; DNA Ligases/genetics; DNA Ligases/metabolism; DNA-Binding Proteins/metabolism; Enzyme Activation; Humans; Mammals; Mutation; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Recombination, Genetic; Transfection

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:DNLI4

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q13426

F

Seeded From UniProt

complete

HUMAN:DNLI4

involved_in

GO:0006302: double-strand break repair

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:DNLI4

enables

GO:0016874: ligase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:XRCC4

part_of

GO:0032807: DNA ligase IV complex

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

HUMAN:XRCC4

NOT|enables

GO:0016874: ligase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

HUMAN:XRCC4

involved_in

GO:0010165: response to X-ray

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:XRCC4

involved_in

GO:0006302: double-strand break repair

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

HUMAN:XRCC4

involved_in

GO:0051351: positive regulation of ligase activity

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete


See also

References

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