Structure-function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation - Wikidata - awgldk - TriplyDB

Structure-function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation

Structure-function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation

http://www.wikidata.org/entity/Q27671587

about

Structural insights into the unique single-stranded DNA-binding mode of Helicobacter pylori DprA Structural insights into the dimerization of the response regulator ComE from Streptococcus pneumoniae Comparative proteomic analysis of Neisseria meningitidis wildtype and dprA null mutant strains links DNA processing to pilus biogenesis.Bacterial RadA is a DnaB-type helicase interacting with RecA to promote bidirectional D-loop extension Evidence that the C-terminal domain of a type B PutA protein contributes to aldehyde dehydrogenase activity and substrate channeling.Staphylococcus aureus competence genes: mapping of the SigH, ComK1 and ComK2 regulons by transcriptome sequencing.RecFOR is not required for pneumococcal transformation but together with XerS for resolution of chromosome dimers frequently formed in the process.Natural genetic transformation generates a population of merodiploids in Streptococcus pneumoniae Insights into the Functional Roles of N-Terminal and C-Terminal Domains of Helicobacter pylori DprA Epigenetic Switch Driven by DNA Inversions Dictates Phase Variation in Streptococcus pneumoniae.Costs and benefits of natural transformation in Acinetobacter baylyi.Direct involvement of DprA, the transformation-dedicated RecA loader, in the shut-off of pneumococcal competence.Natural competence and the evolution of DNA uptake specificity.Helicobacter pylori DprA alleviates restriction barrier for incoming DNA Comprehensive Transcriptome Profiles of Streptococcus mutans UA159 Map Core Streptococcal Competence Genes.Uptake of extracellular DNA: competence induced pili in natural transformation of Streptococcus pneumoniae.Molecular determinants of the DprA-RecA interaction for nucleation on ssDNA.Modeling the ComD/ComE/comcde interaction network using small angle X-ray scattering.No effect of natural transformation on the evolution of resistance to bacteriophages in the Acinetobacter baylyi model system.Roles of Bacillus subtilis DprA and SsbA in RecA-mediated genetic recombination.DprA from Neisseria meningitidis: properties and role in natural competence for transformation.Bacterial transformation: ComFA is a DNA-dependent ATPase that forms complexes with ComFC and DprA.A visual review of the human pathogen Streptococcus pneumoniae.Rhodobacter capsulatus DprA is essential for RecA-mediated gene transfer agent (RcGTA) recipient capability regulated by quorum-sensing and the CtrA response regulator.

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Structure-function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation

http://www.wikidata.org/entity/Q27671587

description

2012 nî lūn-bûn

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2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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Proceedings of the National Academy of Sciences of the United States of America

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Structure-function analysis of ...... onto DNA during transformation

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Anne-Lise Soulet

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Bernard Martin

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Dominique Durand

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Herman van Tilbeurgh

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Isabelle Mortier-Barrière

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Jean-Pierre Claverys

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Marie-Françoise Noirot-Gros

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Nathalie Campo

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Patrice Polard

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Philippe Noirot

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P2860

The Significance of Pneumococcal Types

Insights into DNA recombination from the structure of a RAD51-BRCA2 complex

TM-align: a protein structure alignment algorithm based on the TM-score

Structure of the single-strand annealing domain of human RAD52 protein

Identification of a new regulator in Streptococcus pneumoniae linking quorum sensing to competence for genetic transformation

An unmodified heptadecapeptide pheromone induces competence for genetic transformation in Streptococcus pneumoniae

RecBCD enzyme and the repair of double-stranded DNA breaks

Genetic analysis of the capsular biosynthetic locus from all 90 pneumococcal serotypes.

Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins

The SAM domain of polyhomeotic forms a helical polymer

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37

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109

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Nicolas Mirouze

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230699049

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22904190

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protein structure

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3443122

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