Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair - sprookjes - yvandenbroek - TriplyDB

Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair

Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair

http://www.wikidata.org/entity/Q28486710

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Simultaneous analysis of multiple Mycobacterium tuberculosis knockdown mutants in vitro and in vivo Functional characterization of UvrD helicases from Haemophilus influenzae and Helicobacter pylori The minimal Bacillus subtilis nonhomologous end joining repair machinery A Sir2-like protein participates in mycobacterial NHEJ Enzymatic activities and DNA substrate specificity of Mycobacterium tuberculosis DNA helicase XPB AdnAB: a new DSB-resecting motor-nuclease from mycobacteria.Characterization of the mycobacterial AdnAB DNA motor provides insights into the evolution of bacterial motor-nuclease machines Catalytic and non-catalytic roles for the mono-ADP-ribosyltransferase Arr in the mycobacterial DNA damage response.Characterization of three mycobacterial DinB (DNA polymerase IV) paralogs highlights DinB2 as naturally adept at ribonucleotide incorporation.A conserved helicase processivity factor is needed for conjugation and replication of an integrative and conjugative element Regulated Expression Systems for Mycobacteria and Their Applications Plasmodium falciparum UvrD activities are downregulated by DNA-interacting compounds and its dsRNA inhibits malaria parasite growth UvrD2 is essential in Mycobacterium tuberculosis, but its helicase activity is not required.Comparative Genomics of Field Isolates of Mycobacterium bovis and M. caprae Provides Evidence for Possible Correlates with Bacterial Viability and Virulence.Mycobacterium smegmatis HelY Is an RNA-Activated ATPase/dATPase and 3'-to-5' Helicase That Unwinds 3'-Tailed RNA Duplexes and RNA:DNA Hybrids.Mycobacterium smegmatis RqlH defines a novel clade of bacterial RecQ-like DNA helicases with ATP-dependent 3'-5' translocase and duplex unwinding activities Mycobacterium smegmatis SftH exemplifies a distinctive clade of superfamily II DNA-dependent ATPases with 3' to 5' translocase and helicase activities Mycobacterium smegmatis Lhr Is a DNA-dependent ATPase and a 3'-to-5' DNA translocase and helicase that prefers to unwind 3'-tailed RNA:DNA hybrids C-terminal region of bacterial Ku controls DNA bridging, DNA threading and recruitment of DNA ligase D for double strand breaks repair Characterization of the mycobacterial NER system reveals novel functions of the uvrD1 helicase Domain requirements for DNA unwinding by mycobacterial UvrD2, an essential DNA helicase.Site-2 protease substrate specificity and coupling in trans by a PDZ-substrate adapter protein.Mutational analysis of Mycobacterium UvrD1 identifies functional groups required for ATP hydrolysis, DNA unwinding, and chemomechanical coupling DNA repair in Mycobacterium tuberculosis revisited.Division of labor among Mycobacterium smegmatis RNase H enzymes: RNase H1 activity of RnhA or RnhC is essential for growth whereas RnhB and RnhA guard against killing by hydrogen peroxide in stationary phase.DNA repair systems and the pathogenesis of Mycobacterium tuberculosis: varying activities at different stages of infection.The unstructured C-terminal extension of UvrD interacts with UvrB, but is dispensable for nucleotide excision repair.Genome Wide In silico Analysis of the Mismatch Repair Components of Plasmodium falciparum and Their Comparison with Human Host.Mycobacterium tuberculosis and Mycobacterium marinum non-homologous end-joining proteins can function together to join DNA ends in Escherichia coli.Structure of mycobacterial 3'-to-5' RNA:DNA helicase Lhr bound to a ssDNA tracking strand highlights distinctive features of a novel family of bacterial helicases.Superfamily I helicases as modular components of DNA-processing machines.

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Mycobacterial UvrD1 is a Ku-dependent DNA helicase that plays a role in multiple DNA repair events, including double-strand break repair

http://www.wikidata.org/entity/Q28486710

description

2007 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի մայիսին հրատարակված գիտական հոդված

@hy

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

artículu científicu espublizáu en 2007

@ast

im Mai 2007 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 2007/05/18)

@sk

vědecký článek publikovaný v roce 2007

@cs

wetenschappelijk artikel (gepubliceerd op 2007/05/18)

@nl

наукова стаття, опублікована в травні 2007

@uk

name

Mycobacterial UvrD1 is a Ku-de ...... ing double-strand break repair

@ast

Mycobacterial UvrD1 is a Ku-de ...... ing double-strand break repair

@en

Mycobacterial UvrD1 is a Ku-de ...... ing double-strand break repair

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type

label

Mycobacterial UvrD1 is a Ku-de ...... ing double-strand break repair

@ast

Mycobacterial UvrD1 is a Ku-de ...... ing double-strand break repair

@en

Mycobacterial UvrD1 is a Ku-de ...... ing double-strand break repair

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prefLabel

Mycobacterial UvrD1 is a Ku-de ...... ing double-strand break repair

@ast

Mycobacterial UvrD1 is a Ku-de ...... ing double-strand break repair

@en

Mycobacterial UvrD1 is a Ku-de ...... ing double-strand break repair

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P1433

Journal of Biological Chemistry

P1476

Mycobacterial UvrD1 is a Ku-de ...... ing double-strand break repair

@en

P2093

Feng Gao

http://www.w3.org/2001/XMLSchema#string

Krishna Murari Sinha

http://www.w3.org/2001/XMLSchema#string

Michael S. Glickman

http://www.w3.org/2001/XMLSchema#string

Nicolas C. Stephanou

http://www.w3.org/2001/XMLSchema#string

Stewart Shuman

http://www.w3.org/2001/XMLSchema#string

P2860

A functional interaction of Ku with Werner exonuclease facilitates digestion of damaged DNA

Identification and biochemical characterization of a Werner's syndrome protein complex with Ku70/80 and poly(ADP-ribose) polymerase-1

Ku heterodimer binds to both ends of the Werner protein and functional interaction occurs at the Werner N-terminus

Controlling gene expression in mycobacteria with anhydrotetracycline and Tet repressor

A conserved and species-specific functional interaction between the Werner syndrome-like exonuclease atWEX and the Ku heterodimer in Arabidopsis

Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair

UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke

Functional interaction between Ku and the werner syndrome protein in DNA end processing

Roles of nonhomologous DNA end joining, V(D)J recombination, and class switch recombination in chromosomal translocations

Identification of a DNA nonhomologous end-joining complex in bacteria

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15114–15125

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scholarly article

P356

10.1074/JBC.M701167200

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P407

P433

20

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282

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P577

2007-05-18T00:00:00Z

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P698

17376770

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