RT info:eu-repo/semantics/article
T1 The tail of the ParG DNA segregation protein remodels ParF polymers and enhances ATP hydrolysis via an arginine finger-like motif.
Barillà D, Carmelo E, Hayes F.
Proc Natl Acad Sci U S A. 2007 Feb 6;104(6):1811-6. doi: 10.1073/pnas.0607216104. Epub 2007 Jan 29.
PMID: 17261809
A1 Carmelo, Emma
A1 Barillà, Daniela
A1 Hayes, Finbarr
A2 Obstetricia y GinecologíaPediatría, Medicina Preventiva y Salud Pública, Toxicología y Medicina Legal y Forense y Parasitología
A2 Investigación en Parasitología
K1 ParA superfamily
K1 polymerization
K1 plasmid partition
K1 ATPase
AB The ParF protein of plasmid TP228 belongs to the ubiquitous superfamily of ParA ATPases that drive DNA segregation in bacteria. ATP-bound ParF polymerizes into multistranded filaments. The partner protein ParG is dimeric, consisting of C-termini that interweave into a ribbon–helix–helix domain contacting the centromeric DNA and unstructured N-termini. ParG stimulates ATP hydrolysis by ParF 30-fold. Here, we establish that the mobile tails of ParG are crucial for this enhancement and that arginine R19 within the tail is absolutely required for activation of ParF nucleotide hydrolysis. R19 is part of an arginine finger-like loop in ParG that is predicted to intercalate into the ParF nucleotide-binding pocket thereby promotingATPhydrolysis. Significantly, mutations of R19 abrogated DNA segregation in vivo, proving that intracellular stimulation of ATP hydrolysis by ParG is a key regulatory process for partitioning. Furthermore, ParG bundles ParF-ATP filaments as well as promoting nucleotide-independent polymerization. The N-terminal flexible tail is required for both activities, because N-terminal ParG polypeptides are defective in both functions. Strikingly, the critical arginine finger-like residue R19 is dispensable for ParG-mediated remodeling of ParF polymers, revealing that the ParG N-terminal tail possesses two separable activities in the interplay with ParF: a catalytic function during ATP hydrolysis and a mechanical role in modulation of polymerization. We speculate that activation of nucleotide hydrolysis via an arginine finger loop may be a conserved, regulatory mechanism of ParA family members and their partner proteins, including ParAParB and Soj-Spo0J that mediate DNA segregation and MinD-MinE that determine septum localization.
YR 2007
FD 2007
LK http://riull.ull.es/xmlui/handle/915/37281
UL http://riull.ull.es/xmlui/handle/915/37281
LA en
NO Revista: Proceedings of the National Academy of Sciences of the United States of AmericaISSN: 0027-8424Año de publicación: 2007Volumen: 104Número: 6Páginas: 1811-1816Tipo: Artículo
DS Repositorio institucional de la Universidad de La Laguna
RD 17-jun-2024