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

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

Volumn 109, Issue 37, 2012, Pages

  Quevillon Cheruel, Sophie ^a   Campo, Nathalie ^b,c   Mirouze, Nicolas ^b,c,d   Mortier Barrière, Isabelle ^b,c   Brooks, Mark A ^a   Boudes, Marion ^a   Durand, Dominique ^a   Soulet, Anne Lise ^b,c   Lisboa, Johnny ^a   Noirot, Philippe ^d   Martin, Bernard ^b,c   Van Tilbeurgh, Herman ^a   Noirot Gros, Marie Françoise ^d   Claverys, Jean Pierre ^b,c   Polard, Patrice ^b,c  

^a INSTITUTE FOR INTEGRATIVE BIOLOGY OF THE CELL I2BC   (France)

^b CNRS   (France)

^c UNIVERSITÉ PAUL SABATIER   (France)

^d UMR1319 MICALIS   (France)

Author keywords

Bacterial transformation; Genetic exchange; Horizontal gene transfer; Recombinase loader; Recombination mediator protein

Indexed keywords

BACTERIAL PROTEIN; DIMER; DNA; PROTEIN DPRA; RECA PROTEIN; SSDNA; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL CELL; BACTERIAL GENETICS; BACTERIUM MUTANT; BACTERIUM TRANSFORMATION; COMPLEX FORMATION; DIMERIZATION; IN VITRO STUDY; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STREPTOCOCCUS PNEUMONIAE;

BACTERIAL PROTEINS; BLOTTING, WESTERN; CRYSTALLIZATION; DIMERIZATION; DNA; DNA PRIMERS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; REC A RECOMBINASES; STREPTOCOCCUS PNEUMONIAE; TRANSFORMATION, BACTERIAL; TWO-HYBRID SYSTEM TECHNIQUES;

BACTERIA (MICROORGANISMS); POSIBACTERIA; STREPTOCOCCUS PNEUMONIAE;

EID: 84866295476     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1205638109     Document Type: Article

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