Structure-function analysis of pneumococcal DprA protein reveals that dimerization is crucial for loading RecA recombinase onto DNA during transformation-Reference-Cited by-同舟云学术

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

Published:2012-08-17 Issue:37 Volume:109 Page:E2466-E2475
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Quevillon-Cheruel S.,Campo N.,Mirouze N.,Mortier-Barriere I.,Brooks M. A.,Boudes M.,Durand D.,Soulet A.-L.,Lisboa J.,Noirot P.,Martin B.,van Tilbeurgh H.,Noirot-Gros M.-F.,Claverys J.-P.,Polard P.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference37 articles.

1. Motoring along with the bacterial RecA protein

2. RecA family proteins in archaea: RadA and its cousins

3. RMPs: recombination/replication mediator proteins

4. RecBCD Enzyme and the Repair of Double-Stranded DNA Breaks

5. rexAB mutants in Streptococcus pneumoniae

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