Biochemical and genetic analysis of the four DNA ligases of mycobacteria
about
Mycobacterium tuberculosis NAD+-dependent DNA ligase is selectively inhibited by glycosylamines compared with human DNA ligase IMaking ends meet: repairing breaks in bacterial DNA by non-homologous end-joiningStructural basis for nick recognition by a minimal pluripotent DNA ligaseStructure of a NHEJ polymerase-mediated DNA synaptic complexSolution structure and DNA-binding properties of the phosphoesterase domain of DNA ligase DM. tuberculosis Sliding β-Clamp Does Not Interact Directly with the NAD+ -Dependent DNA LigaseMycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repairThe minimal Bacillus subtilis nonhomologous end joining repair machineryA primer-dependent polymerase function of pseudomonas aeruginosa ATP-dependent DNA ligase (LigD)Novel 3'-ribonuclease and 3'-phosphatase activities of the bacterial non-homologous end-joining protein, DNA ligase DMechanism of nonhomologous end-joining in mycobacteria: a low-fidelity repair system driven by Ku, ligase D and ligase CNAD+-dependent DNA Ligase (Rv3014c) from Mycobacterium tuberculosis. Crystal structure of the adenylation domain and identification of novel inhibitors.Identification and characterization of an inhibitor specific to bacterial NAD+-dependent DNA ligases.AdnAB: a new DSB-resecting motor-nuclease from mycobacteria.Deficiency of double-strand DNA break repair does not impair Mycobacterium tuberculosis virulence in multiple animal models of infection.Characterization of the roles of the catalytic domains of Mycobacterium tuberculosis ligase D in Ku-dependent error-prone DNA end joiningMycobacteria exploit three genetically distinct DNA double-strand break repair pathwaysCharacterization of three mycobacterial DinB (DNA polymerase IV) paralogs highlights DinB2 as naturally adept at ribonucleotide incorporation.Enzyme-adenylate structure of a bacterial ATP-dependent DNA ligase with a minimized DNA-binding surface.Atomic structure and nonhomologous end-joining function of the polymerase component of bacterial DNA ligase DDirect and inverted repeats elicit genetic instability by both exploiting and eluding DNA double-strand break repair systems in mycobacteria.Identification of a chemical that inhibits the mycobacterial UvrABC complex in nucleotide excision repairDynamics of phosphodiester synthesis by DNA ligaseChromatin organization and radio resistance in the bacterium Gemmata obscuriglobus.The pathways and outcomes of mycobacterial NHEJ depend on the structure of the broken DNA endsA dual role for mycobacterial RecO in RecA-dependent homologous recombination and RecA-independent single-strand annealing.Mechanistic flexibility as a conserved theme across 3 billion years of nonhomologous DNA end-joining.Domain requirements for DNA unwinding by mycobacterial UvrD2, an essential DNA helicase.Characterization of Mycobacterium smegmatis PolD2 and PolD1 as RNA/DNA polymerases homologous to the POL domain of bacterial DNA ligase D.Multiple and Variable NHEJ-Like Genes Are Involved in Resistance to DNA Damage in Streptomyces ambofaciens.DNA repair in Mycobacterium tuberculosis revisited.Discovery and design of DNA and RNA ligase inhibitors in infectious microorganisms.Is Mycobacterium tuberculosis stressed out? A critical assessment of the genetic evidence.Protein targets for structure-based anti-Mycobacterium tuberculosis drug discovery.Expression of Mycobacterium tuberculosis Ku and Ligase D in Escherichia coli results in RecA and RecB-independent DNA end-joining at regions of microhomology.Substrate specificity and structure-function analysis of the 3'-phosphoesterase component of the bacterial NHEJ protein, DNA ligase D.Mechanistic assessment of DNA ligase as an antibacterial target in Staphylococcus aureus.The novel Pseudomonas putida plasmid p12969-2 harbors an In127-carrying multidrug-resistant region.Identification of a conserved 5'-dRP lyase activity in bacterial DNA repair ligase D and its potential role in base excision repair.Mycobacterium tuberculosis RecA is indispensable for inhibition of the mitogen-activated protein kinase-dependent bactericidal activity of THP-1-derived macrophages in vitro.
P2860
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P2860
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
description
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2004
@ast
im Mai 2004 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2004/05/14)
@sk
vědecký článek publikovaný v roce 2004
@cs
wetenschappelijk artikel (gepubliceerd op 2004/05/14)
@nl
наукова стаття, опублікована в травні 2004
@uk
name
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
@ast
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
@en
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
@nl
type
label
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
@ast
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
@en
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
@nl
prefLabel
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
@ast
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
@en
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
@nl
P2093
P2860
P356
P1476
Biochemical and genetic analysis of the four DNA ligases of mycobacteria
@en
P2093
Alexandra Martins
Chunling Gong
Michael Glickman
Paola Bongiorno
Stewart Shuman
P2860
P304
20594–20606
P356
10.1074/JBC.M401841200
P407
P577
2004-05-14T00:00:00Z