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DNA ligase IV (LIG4) is not essential for telomere joining.
This study shown that both ligase IV and XRCC4 (show XRCC4 Proteins) may act in concert to modulate the development of glioma.
We demonstrated an association between six previously published single nucleotide polymorphisms (rs15869 [ BRCA2 (show BRCA2 Proteins)], rs1805389 [ LIG4], rs8079544 [ TP53 (show TP53 Proteins)], rs25489 [ XRCC1 (show XRCC1 Proteins)], rs1673041 [ POLD1 (show POLD1 Proteins)], and rs11615 [ ERCC1 (show ERCC1 Proteins)]) and subsequent CNS tumors in survivors of childhood cancer treated by radiation therapy.
In a recombinant PNKP (show PNKP Proteins)-XRCC4 (show XRCC4 Proteins)-LigIV complex, both the PNKP (show PNKP Proteins) FHA (show CRY2 Proteins) and catalytic domains contact the XRCC4 (show XRCC4 Proteins) coiled-coil and LigIV BRCT repeats. Multipoint contacts between PNKP (show PNKP Proteins) and XRCC4 (show XRCC4 Proteins)-LigIV regulate PNKP (show PNKP Proteins) recruitment and activity within NHEJ.
Data suggest that stimulation of Artemis nuclease/DCLRE1C (show DCLRE1C Proteins) activity by XRCC4 (show XRCC4 Proteins)-DNA ligase IV hetero-complex and efficiency of blunt-end ligation are determined by structural configurations at the DNA ends. (XRCC4 (show XRCC4 Proteins) = X-ray repair cross complementing 4)
found that the rs228593, rs2267437 and rs1805388 functional polymorphisms probably alter the level of expression of the ATM (show ATM Proteins), XRCC6 (show XRCC6 Proteins) and LIG4 genes, respectively, being important in the maintenance of genomic instability in MDS (show PAFAH1B1 Proteins)
marked overlap of dyskeratosis congenita with four other genetic syndromes, confounding accurate diagnosis and subsequent management. Patients with clinical features of dyskeratosis congenita need to have genetic analysis of USB1 (show USB1 Proteins), LIG4 and GRHL2 (show GRHL2 Proteins) in addition to the classical dyskeratosis congenita genes and telomere length measurements.
The rs1805388 in LIG4 was associated with increased radioresistance.
LIG4 is highly upregulated in human colorectal cancer cells.
Five novel mutations in LIG4 and a potential hotspot mutation (c.833G > T; p.R278L) in the Chinese population with LIG4 deficiency syndrome were identified.
Our study identifies LIG4 as a predictor of an increased risk for early biochemical recurrence in prostate cancer
The data firmly demonstrate Lig4(R278H) activity renders nonhomologous end-joining (NHEJ) DNA repair to be more error-prone, and predict increased error-prone NHEJ and A-EJ suppression as the cause of defective B lymphopoiesis in Lig4 patients.
To promote homology-directed r at the expense of nonhomologous end joining , we targeted DNA ligase IV, a key enzyme in the NHEJ pathway, using the inhibitor Scr7. This approach should be applicable to other customizable endonucleases
Lig4 and XRCC1 (show XRCC1 Proteins) double-deficient cells switch as efficiently as Lig4-deficient cells, clearly indicating that XRCC1 (show XRCC1 Proteins) is dispensable for A-EJ in CH12F3 cells during class switch recombination
These studies provide insight into the interplay between DNA damage responses in the developing brain and the DNA ligase IV plat (show PLAT Proteins) the role in repairing endogenously arising DNA double-strand breaks.
Lig4-deficient B cells have reduced, but still substantial, immunoglobulins class switch recombination
Homozygous DNA ligase IV R278H mutation in mice leads to leaky SCID (show PRKDC Proteins) and represents a model for human LIG4 syndrome.
Lig4 and Rad54 (show RAD54L Proteins) cooperate to support cellular proliferation, dna repair, and prevent chromosome and single chromatid aberrations
LIG4 mutations can result in either a developmental defect with immunological abnormalities or a severe combined immunodeficiency (show PRKDC Proteins) picture with normal development.
DNA Ligase IV is engaged in extrachromosomal circular major satellite DNA synthesis
DNA-PK kinase activity results in disassembly of the Ku/DNA ligase IV/Xrcc4 (show XRCC4 Proteins) complex
The protein encoded by this gene is a DNA ligase that joins single-strand breaks in a double-stranded polydeoxynucleotide in an ATP-dependent reaction. This protein is essential for V(D)J recombination and DNA double-strand break (DSB) repair through nonhomologous end joining (NHEJ). This protein forms a complex with the X-ray repair cross complementing protein 4 (XRCC4), and further interacts with the DNA-dependent protein kinase (DNA-PK). Both XRCC4 and DNA-PK are known to be required for NHEJ. The crystal structure of the complex formed by this protein and XRCC4 has been resolved. Defects in this gene are the cause of LIG4 syndrome. Alternatively spliced transcript variants encoding the same protein have been observed.
DNA ligase 4
, ligase IV, DNA, ATP-dependent
, DNA ligase IV
, DNA ligase (ATP) 4
, ligase4-like protein
, DNA ligase 4-like
, dsDNA break repair ligase
, polydeoxyribonucleotide synthase [ATP] 4
, DNA joinase
, DNA repair enzyme
, polynucleotide ligase