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Bacterial transformation: ComFA is a DNA‐dependent ATPase that forms complexes with ComFC and DprA
Author(s) -
Diallo Amy,
Foster Hannah R.,
Gromek Katarzyna A.,
Perry Thomas N.,
Dujeancourt Annick,
Krasteva Petya V.,
Gubellini Francesca,
Falbel Tanya G.,
Burton Briana M.,
Fronzes Rémi
Publication year - 2017
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13732
Subject(s) - transformation (genetics) , biology , dna , operon , homologous recombination , streptococcus pneumoniae , recombination , genetics , dna repair , genomic dna , computational biology , gene , bacteria , escherichia coli
Summary Pneumococcal natural transformation contributes to genomic plasticity, antibiotic resistance development and vaccine escape. Streptococcus pneumoniae , like many other naturally transformable species, has evolved sophisticated protein machinery for the binding and uptake of DNA. Two proteins encoded by the comF operon, ComFA and ComFC, are involved in transformation but their exact molecular roles remain unknown. In this study, we provide experimental evidence that ComFA binds to single stranded DNA (ssDNA) and has ssDNA‐dependent ATPase activity. We show that both ComFA and ComFC are essential for the transformation process in pneumococci. Moreover, we show that these proteins interact with each other and with other proteins involved in homologous recombination, such as DprA, thus placing the ComFA‐ComFC duo at the interface between DNA uptake and DNA recombination during transformation.