The tail of the ParG DNA segregation protein remodels ParF polymers and enhances ATP hydrolysis via an arginine finger-like motif

• DOI: 10.1073/pnas.0607216104
• Publication Date: 2007-02-02T18:37:31Z
• Authors: Daniela Barillà; Emma Carmelo; Finbarr Hayes
• Keywords: Walker motifs

The ParF protein of plasmid TP228 belongs to the ubiquitous superfamily ParA ATPases that drive DNA segregation in bacteria. ATP-bound polymerizes into multistranded filaments. partner ParG is dimeric, consisting C-termini interweave a ribbon–helix–helix domain contacting centromeric and unstructured N-termini. stimulates ATP hydrolysis by ≈30-fold. Here, we establish mobile tails are crucial for this enhancement arginine R19 within tail absolutely required activation nucleotide hydrolysis. part an finger-like loop predicted intercalate nucleotide-binding pocket thereby promoting Significantly, mutations abrogated vivo , proving intracellular stimulation key regulatory process partitioning. Furthermore, bundles ParF-ATP filaments as well nucleotide-independent polymerization. N-terminal flexible both activities, because ΔParG polypeptides defective functions. Strikingly, critical residue dispensable ParG-mediated remodeling polymers, revealing possesses two separable activities interplay with ParF: catalytic function during mechanical role modulation We speculate via finger may be conserved, mechanism family members their proteins, including ParA-ParB Soj-Spo0J mediate MinD-MinE determine septum localization.