Results 21 to 30 of about 1,712,707 (295)

Bacterial DNA ligases [PDF]

open access: yesMolecular Microbiology, 2001
DNA ligases join breaks in the phosphodiester backbone of DNA molecules and are used in many essential reactions within the cell. All DNA ligases follow the same reaction mechanism, but they may use either ATP or NAD+ as a cofactor. All Bacteria (eubacteria) contain NAD+‐dependent DNA ligases, and the uniqueness of these enzymes to Bacteria makes them ...
Wilkinson, A, Day, J, Bowater, R
openaire   +3 more sources

Structures of LIG1 that engage with mutagenic mismatches inserted by polβ in base excision repair

open access: yesNature Communications, 2022
Ligase I seals two ends of DNA during DNA repair and replication. Here — solving structures of Ligase I with imperfect DNA harboring mismatches incorporated by DNA polymerase — the authors reveal how the repair proteins maintain fidelity at final ...
Qun Tang   +3 more
doaj   +1 more source

High-fidelity DNA ligation enforces accurate Okazaki fragment maturation during DNA replication

open access: yesNature Communications, 2021
DNA ligase 1 (LIG1) finalizes eukaryotic nuclear DNA synthesis by sealing Okazaki fragments using DNA end-joining reactions. Here the authors, by studying an engineered low-fidelity LIG1, reveal that LIG1 is a highly accurate DNA ligase in vivo.
Jessica S. Williams   +5 more
doaj   +1 more source

MAMMALIAN DNA LIGASES [PDF]

open access: yesAnnual Review of Biochemistry, 1992
DNA LIGASE I .... ... ....... ...... . . . . . .. . . . .. ........ . 255 Structure. . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 255 Gene Structure and Chromosome Mapping . . . . ......... . . . . . .. . . . . .
T, Lindahl, D E, Barnes
openaire   +2 more sources

Differential requirement for BRCA1-BARD1 E3 ubiquitin ligase activity in DNA damage repair and meiosis in the Caenorhabditis elegans germ line.

open access: yesPLoS Genetics, 2023
The tumor suppressor BRCA1-BARD1 complex regulates many cellular processes; of critical importance to its tumor suppressor function is its role in genome integrity.
Qianyan Li   +4 more
doaj   +1 more source

Thermostable DNA ligases from hyperthermophiles in biotechnology

open access: yesFrontiers in Microbiology, 2023
DNA ligase is an important enzyme ubiquitous in all three kingdoms of life that can ligate DNA strands, thus playing essential roles in DNA replication, repair and recombination in vivo.
Jingru Shi   +3 more
doaj   +1 more source

DNA Ligase I, the Replicative DNA Ligase [PDF]

open access: yes, 2012
Multiple DNA ligation events are required to join the Okazaki fragments generated during lagging strand DNA synthesis. In eukaryotes, this is primarily carried out by members of the DNA ligase I family. The C-terminal catalytic region of these enzymes is composed of three domains: a DNA binding domain, an adenylation domain and an OB-fold domain.
Timothy R L, Howes, Alan E, Tomkinson
openaire   +2 more sources

BRCA1 is a histone-H2A-specific ubiquitin ligase [PDF]

open access: yes, 2014
The RING domain proteins BRCA1 and BARD1 comprise a heterodimeric ubiquitin (E3) ligase that is required for the accumulation of ubiquitin conjugates at sites of DNA damage and for silencing at DNA satellite repeat regions. Despite its links to chromatin,
Donna L. Mallery   +15 more
core   +1 more source

Identification of the DNA repair defects in a case of Dubowitz syndrome. [PDF]

open access: yesPLoS ONE, 2013
Dubowitz Syndrome is an autosomal recessive disorder with a unique set of clinical features including microcephaly and susceptibility to tumor formation. Although more than 140 cases of Dubowitz syndrome have been reported since 1965, the genetic defects
Jingyin Yue   +6 more
doaj   +1 more source

Impact of DNA ligase IV on nonhomologous end joining pathways during class switch recombination in human cells [PDF]

open access: yes, 2005
Class switch recombination (CSR) is a region-specific, transcriptionally regulated, nonhomologous recombinational process that is initiated by activation-induced cytidine deaminase (AID).
Lennart Hammarström   +16 more
core   +1 more source

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