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• W1979289218 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. Conjugative plasmids block translocation of rival plasmids using fertility inhibition factors (FINs). Here Maindola et al.present the structure of the FIN Osa and show that it contains a ParB/Sulfiredoxin fold with both ATPase and DNase activity, with general functional implications for this fold." @default.
• W1979289218 created "2016-06-24" @default.
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• W1979289218 date "2014-10-31" @default.
• W1979289218 modified "2023-09-28" @default.
• W1979289218 title "Multiple enzymatic activities of ParB/Srx superfamily mediate sexual conflict among conjugative plasmids" @default.
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• W1979289218 doi "https://doi.org/10.1038/ncomms6322" @default.
• W1979289218 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4241021" @default.
• W1979289218 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25358815" @default.
• W1979289218 hasPublicationYear "2014" @default.
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