Multiple enzymatic activities of ParB/Srx superfamily mediate sexual conflict among conjugative plasmids

Priyank Maindola, Rahul Raina, Parveen Goyal, Krishnamohan Atmakuri, Abhishek Ojha, Sourabh Gupta, Peter J. Christie, Lakshminarayan M. Iyer, L. Aravind () and Arulandu Arockiasamy ()
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Priyank Maindola: Structural and Computational Biology Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg
Rahul Raina: Structural and Computational Biology Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg
Parveen Goyal: Structural and Computational Biology Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg
Krishnamohan Atmakuri: University of Texas Medical School at Houston
Abhishek Ojha: Structural and Computational Biology Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg
Sourabh Gupta: Structural and Computational Biology Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg
Peter J. Christie: University of Texas Medical School at Houston
Lakshminarayan M. Iyer: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
L. Aravind: National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
Arulandu Arockiasamy: Structural and Computational Biology Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Marg

Nature Communications, 2014, vol. 5, issue 1, 1-11

Abstract: Abstract Conjugative plasmids are typically locked in intergenomic and sexual conflicts with co-resident rivals, whose translocation they block using fertility inhibition factors (FINs). We describe here the first crystal structure of an enigmatic FIN Osa deployed by the proteobacterial plasmid pSa. Osa contains a catalytically active version of the ParB/Sulfiredoxin fold with both ATPase and DNase activity, the latter being regulated by an ATP-dependent switch. Using the Agrobacterium tumefaciens VirB/D4 type IV secretion system (T4SS), a relative of the conjugative T4SS, we demonstrate that catalytically active Osa blocks T-DNA transfer into plants. With a partially reconstituted T4SS in vitro, we show that Osa degrades T-DNA in the T-DNA-VirD2 complex before its translocation. Further, we present evidence for conservation and interplay between ATPase and DNase activities throughout the ParB/Sulfiredoxin fold, using other members of the family, namely P1 ParB and RK2 KorB, which have general functional implications across diverse biological contexts.

Date: 2014
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DOI: 10.1038/ncomms6322

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