Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

ATP hydrolysis and DNA binding by the Escherichia coli RecF protein.

The Journal of biological chemistry - 28 May 1999

Webb B L, Cox M M, Inman R B

Abstract excerpt

The Escherichia coli RecF protein possesses a weak ATP hydrolytic activity. ATP hydrolysis leads to RecF dissociation from double-stranded (ds)DNA. The RecF protein is subject to precipitation and an accompanying inactivation in vitro when not bound to DNA. A mutant RecF protein that can bind but cannot hydrolyze ATP (RecF K36R) does not readily dissociate from dsDNA in the presence of ATP. This is in contrast to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adenosine Triphosphatases
Share to Adenosine Triphosphate
Share to DNA, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Hydrogen-Ion Concentration

Share to Microscopy, Electron

Share to Nucleic Acid Conformation

Share to Protein Conformation

Source

Identifiers

PMID: 10336423
DOI: 10.1074/jbc.274.22.15367

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

ATP hydrolysis and DNA binding by the Escherichia coli RecF protein.PMID 10336423Read ↗

Requirements for ATP binding and hydrolysis in RecA function in Escherichia coli.Semantic proximity Read ↗

Purification and biochemical characterization of Escherichia coli RecA proteins mutated in the putative DNA binding site.Semantic proximity Read ↗

Molecular design and functional organization of the RecA protein.Semantic proximity Read ↗

The homologous pairing domain of RecA also mediates the allosteric regulation of DNA binding and ATP hydrolysis: a remarkable concentration of functional residues.Semantic proximity Read ↗

Characterization of RecA1332 in vivo and in vitro. A role for alpha-helix E as a liaison between the subunit-subunit interface and the DNA and ATP binding domains of RecA protein.Semantic proximity Read ↗

Coupling DNA-binding and ATP hydrolysis in Escherichia coli RecQ: role of a highly conserved aromatic-rich sequence.Semantic proximity Read ↗

Biochemical properties of the Escherichia coli recA430 protein. Analysis of a mutation that affects the interaction of the ATP-recA protein complex with single-stranded DNA.Semantic proximity Read ↗

Disassembly of Escherichia coli RecA E38K/DeltaC17 nucleoprotein filaments is required to complete DNA strand exchange.Semantic proximity Read ↗

Structural and functional characterization of oligomeric states of proteins in RecFOR pathway.Semantic proximity Read ↗

RecA filament dynamics during DNA strand exchange reactions.Semantic proximity Read ↗

A recombinational defect in the C-terminal domain of Escherichia coli RecA2278-5 protein is compensated by protein binding to ATP.Semantic proximity Read ↗

Characterization of a mutant RecA protein that facilitates homologous genetic recombination but not recombinational DNA repair: RecA423.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.