scholarly journals DNA Ligase I Deficiency

2020 ◽  
Author(s):  
Keyword(s):  
Dna Ligase ◽  
Dna Ligase I

scholarly journals The human checkpoint sensor and alternative DNA clamp Rad9–Rad1–Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery

2005 ◽  
Vol 389 (1) ◽  
pp. 13-17 ◽  
Author(s):  
Ekaterina SMIRNOVA ◽  
Magali TOUEILLE ◽  
Enni MARKKANEN ◽  
Ulrich HÜBSCHER
Keyword(s):  
Quality Control ◽  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Ligase ◽  
Dna Polymerase Β ◽  
Flap Endonuclease 1 ◽  
Important Target ◽  
Dna Ligase I ◽  
Base Excision

The human checkpoint sensor and alternative clamp Rad9–Rad1–Hus1 can interact with and specifically stimulate DNA ligase I. The very recently described interactions of Rad9–Rad1–Hus1 with MutY DNA glycosylase, DNA polymerase β and Flap endonuclease 1 now complete our view that the long-patch base excision machinery is an important target of the Rad9–Rad1–Hus1 complex, thus enhancing the quality control of DNA.

Cloning and sequence analysis of a cDNA coding for the murine DNA ligase I enzyme

Gene ◽  
1994 ◽  
Vol 144 (2) ◽  
pp. 253-257 ◽  
Author(s):  
Elena Savini ◽  
Giuseppe Biamonti ◽  
Giovanni Ciarrocchi ◽  
Alessandra Montecucco
Keyword(s):  
Sequence Analysis ◽  
Dna Ligase ◽  
Dna Ligase I

scholarly journals Dual mode of inhibition of purified DNA ligase I from human cells by 9-beta-D-arabinofuranosyl-2-fluoroadenine triphosphate.

1992 ◽  
Vol 267 (4) ◽  
pp. 2345-2349 ◽  
Author(s):  
S W Yang ◽  
P Huang ◽  
W Plunkett ◽  
F F Becker ◽  
J Y Chan
Keyword(s):  
Human Cells ◽  
Dna Ligase ◽  
Dual Mode ◽  
Dna Ligase I

scholarly journals Thermodynamics of Human DNA Ligase I Trimerization and Association with DNA Polymerase β

1998 ◽  
Vol 273 (32) ◽  
pp. 20540-20550 ◽  
Author(s):  
Emilios K. Dimitriadis ◽  
Rajendra Prasad ◽  
Mary K. Vaske ◽  
Ling Chen ◽  
Alan E. Tomkinson ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Dna Ligase ◽  
Dna Polymerase Β ◽  
Human Dna ◽  
Dna Ligase I

MAMMALIAN DNA LIGASES; ALTERED DNA LIGASE I IN BLOOM'S SYNDROME

1991 ◽  
pp. 71
Author(s):  
ALAN E. TOMKINSON ◽  
DEBORAH E. BARNES ◽  
KEN-ICHI KODAMA ◽  
EEMA ROBERTS ◽  
GRAHAM DALY ◽  
...  
Keyword(s):  
Dna Ligase ◽  
Bloom's Syndrome ◽  
Dna Ligases ◽  
Bloom’S Syndrome ◽  
Dna Ligase I

scholarly journals The ligation of pol β mismatch insertion products governs the formation of promutagenic base excision DNA repair intermediates

2020 ◽  
Vol 48 (7) ◽  
pp. 3708-3721 ◽  
Author(s):  
Melike Çağlayan
Keyword(s):  
Excision Repair ◽  
Dna Ligase ◽  
Active Site Residues ◽  
Dna Ligases ◽  
Terminal Domain ◽  
Dna Ligase I ◽  
Nucleotide Insertion ◽  
Base Excision ◽  
Ligation Step

Abstract DNA ligase I and DNA ligase III/XRCC1 complex catalyze the ultimate ligation step following DNA polymerase (pol) β nucleotide insertion during base excision repair (BER). Pol β Asn279 and Arg283 are the critical active site residues for the differentiation of an incoming nucleotide and a template base and the N-terminal domain of DNA ligase I mediates its interaction with pol β. Here, we show inefficient ligation of pol β insertion products with mismatched or damaged nucleotides, with the exception of a Watson–Crick-like dGTP insertion opposite T, using BER DNA ligases in vitro. Moreover, pol β N279A and R283A mutants deter the ligation of the promutagenic repair intermediates and the presence of N-terminal domain of DNA ligase I in a coupled reaction governs the channeling of the pol β insertion products. Our results demonstrate that the BER DNA ligases are compromised by subtle changes in all 12 possible noncanonical base pairs at the 3′-end of the nicked repair intermediate. These findings contribute to understanding of how the identity of the mismatch affects the substrate channeling of the repair pathway and the mechanism underlying the coordination between pol β and DNA ligase at the final ligation step to maintain the BER efficiency.

scholarly journals Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination.

1995 ◽  
Vol 15 (6) ◽  
pp. 3206-3216 ◽  
Author(s):  
Y F Wei ◽  
P Robins ◽  
K Carter ◽  
K Caldecott ◽  
D J Pappin ◽  
...  
Keyword(s):  
Dna Repair ◽  
Cdna Clone ◽  
Dna Ligase ◽  
Dna Ligases ◽  
Dna Ligase Iv ◽  
Ligase Iv ◽  
Dna Ligase I ◽  
Cloned Cdna ◽  
Dna Ligase Iii

Three distinct DNA ligases, I to III, have been found previously in mammalian cells, but a cloned cDNA has been identified only for DNA ligase I, an essential enzyme active in DNA replication. A short peptide sequence conserved close to the C terminus of all known eukaryotic DNA ligases was used to search for additional homologous sequences in human cDNA libraries. Two different incomplete cDNA clones that showed partial homology to the conserved peptide were identified. Full-length cDNAs were obtained and expressed by in vitro transcription and translation. The 103-kDa product of one cDNA clone formed a characteristic complex with the XRCC1 DNA repair protein and was identical with the previously described DNA ligase III. DNA ligase III appears closely related to the smaller DNA ligase II. The 96-kDa in vitro translation product of the second cDNA clone was also shown to be an ATP-dependent DNA ligase. A fourth DNA ligase (DNA ligase IV) has been purified from human cells and shown to be identical to the 96-kDa DNA ligase by unique agreement between mass spectrometry data on tryptic peptides from the purified enzyme and the predicted open reading frame of the cloned cDNA. The amino acid sequences of DNA ligases III and IV share a related active-site motif and several short regions of homology with DNA ligase I, other DNA ligases, and RNA capping enzymes. DNA ligases III and IV are encoded by distinct genes located on human chromosomes 17q11.2-12 and 13q33-34, respectively.

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