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

Mutant DnaA proteins defective in duplex opening of oriC, the origin of chromosomal DNA replication in Escherichia coli.

Molecular microbiology - 1 Jan 2000

Takata M, Guo L, Katayama T, Hase M, Seyama Y, Miki T, Sekimizu K

Abstract excerpt

We characterized three mutant DnaA proteins with an amino acid substitution of R334H, R342H and E361G that renders chromosomal replication cold (20 degrees C) sensitive. Each mutant DnaA protein was highly purified from overproducers, and replication activities were assayed in in vitro oriC replication systems. At 30 degrees C, all three mutant proteins exhibited specific activity similar to that seen with the...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Bacterial Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cold Temperature

Share to DNA Replication

Share to Escherichia coli

Share to Origin Recognition Complex

Share to Single-Strand Specific DNA and RNA Endonucleases

Share to Viral Proteins

Source

Identifiers

PMID: 10652106
DOI: 10.1046/j.1365-2958.2000.01722.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutant DnaA proteins defective in duplex opening of oriC, the origin of chromosomal DNA replication in Escherichia coli.PMID 10652106Read ↗

A common mechanism for the ATP-DnaA-dependent formation of open complexes at the replication origin.Semantic proximity Read ↗

The box VII motif of Escherichia coli DnaA protein is required for DnaA oligomerization at the E. coli replication origin.Semantic proximity Read ↗

New non-detrimental DNA-binding mutants of the Escherichia coli initiator protein DnaA.Semantic proximity Read ↗

The A184V missense mutation of the dnaA5 and dnaA46 alleles confers a defect in ATP binding and thermolability in initiation of Escherichia coli DNA replication.Semantic proximity Read ↗

Threonine 435 of Escherichia coli DnaA protein confers sequence-specific DNA binding activity.Semantic proximity Read ↗

Biochemical characterization of Escherichia coli temperature-sensitive dnaB mutants dnaB8, dnaB252, dnaB70, dnaB43, and dnaB454.Semantic proximity Read ↗

Escherichia coli DnaA protein: specific biochemical defects of mutant DnaAs reduce initiation frequency to suppress a temperature-sensitive dnaX mutation.Semantic proximity Read ↗

Substitutions of Conserved Residues in the C-terminal Region of DnaC Cause Thermolability in Helicase Loading.Semantic proximity Read ↗

Mutations in the DnaA binding sites of the replication origin of Escherichia coli.Semantic proximity Read ↗

A comprehensive set of DnaA-box mutations in the replication origin, oriC, of Escherichia coli.Semantic proximity Read ↗

DnaA Protein of Escherichia coli: oligomerization at the E. coli chromosomal origin is required for initiation and involves specific N-terminal amino acids.Semantic proximity Read ↗

Hyperactive initiation of chromosomal replication in vivo and in vitro by a mutant initiator protein, DnaAcos, of Escherichia coli.Semantic proximity Read ↗

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