Results 51 to 60 of about 2,162,763 (370)

Bacteriophage origin of some minimal ATP-dependent DNA ligases: a new structure from Burkholderia pseudomallei with striking similarity to Chlorella virus ligase

open access: yesScientific Reports, 2021
DNA ligases, the enzymes responsible for joining breaks in the phosphodiester backbone of DNA during replication and repair, vary considerably in size and structure.
Jolyn Pan   +4 more
doaj   +1 more source

Pol I DNA polymerases stimulate DNA end-joining by Escherichia coli DNA ligase [PDF]

open access: yes, 2018
© 2018 Klenow and Klentaq are the large fragment domains of the Pol I DNA polymerases from Escherichia coli and Thermus aquaticus, respectively. Herein, we show that both polymerases can significantly stimulate complementary intermolecular end-joining ...
LiCata, Vince J., Yang, Yanling
core   +2 more sources

DNA Ligase 1 is an essential mediator of sister chromatid telomere fusions in G2 cell cycle phase

open access: yesNucleic Acids Research, 2018
Fusion of critically short or damaged telomeres is associated with the genomic rearrangements that support malignant transformation. We have demonstrated the fundamental contribution of DNA ligase 4-dependent classical non-homologous end-joining to long ...
K. Liddiard   +6 more
semanticscholar   +1 more source

ATM mediates oxidative stress-induced dephosphorylation of DNA ligase IIIα [PDF]

open access: yes, 2006
Among the three mammalian genes encoding DNA ligases, only the LIG3 gene does not have a homolog in lower eukaryotes. In somatic mammalian cells, the nuclear form of DNA ligase IIIα forms a stable complex with the DNA repair protein XRCC1 that is also ...
Alan E. Tomkinson   +46 more
core   +2 more sources

Rat liver DNA ligases [PDF]

open access: yesEuropean Journal of Biochemistry, 1992
A novel form of rat liver DNA ligase (molecular mass 100 kDa) can be differentiated from DNA ligase I by several biochemical parameters. It is a more heat‐labile enzyme and unable to join bluntended DNA, even in the presence of poly(ethylene glycol) concentrations which stimulate such joining by DNA ligase I and T4 DNA ligase.
R H Elder   +3 more
openaire   +4 more sources

Fidelity of RNA templated end-joining by chlorella virus DNA ligase and a novel iLock assay with improved direct RNA detection accuracy

open access: yesNucleic Acids Research, 2017
Ligation-based nucleic acid detection methods are primarily limited to DNA, since they exhibit poor performance on RNA. This is attributed to reduced end-joining efficiency and/or fidelity of ligases. Interestingly, chlorella virus DNA ligase (PBCV-1 DNA
T. Krzywkowski, M. Nilsson
semanticscholar   +1 more source

Targeted disruption of the gene encoding DNA ligase IV leads to lethality in embryonic mice [PDF]

open access: yes, 1998
DNA ligase IV is the most recently identified member of a family of enzymes joining DNA strand breaks in mammalian cell nuclei [1,2]. The enzyme occurs in a complex with the XRCC4 gene product [3], an interaction mediated via its unique carboxyl terminus
Barnes, Deborah E.   +4 more
core   +1 more source

The Action of DNA Ligase at Abasic Sites in DNA [PDF]

open access: yesJournal of Biological Chemistry, 1998
Apurinic/apyrimidinic (AP) sites occur frequently in DNA as a result of spontaneous base loss or following removal of a damaged base by a DNA glycosylase. The action of many AP endonuclease enzymes at abasic sites in DNA leaves a 5'-deoxyribose phosphate (dRP) residue that must be removed during the base excision repair process.
Daniel F. Bogenhagen, Kevin G. Pinz
openaire   +2 more sources

Specific recognition of a multiply phosphorylated motif in the DNA repair scaffold XRCC1 by the FHA domain of human PNK. [PDF]

open access: yes, 2009
Short-patch repair of DNA single-strand breaks and gaps (SSB) is coordinated by XRCC1, a scaffold protein that recruits the DNA polymerase and DNA ligase required for filling and sealing the damaged strand.
Ali, Ammar A. E.   +3 more
core   +3 more sources

Closing the gap on DNA ligase [PDF]

open access: yesStructure, 1996
The crystal structure of T7 DNA ligase complexed with ATP illuminates the mechanism of covalent catalysis by a superfamily of nucleotidyl transferases that includes the ATP-dependent polynucleotide ligases and the GTP-dependent mRNA capping enzymes.
openaire   +3 more sources

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