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

Mutations in the Res subunit of the EcoPI restriction enzyme that affect ATP-dependent reactions.

Journal of molecular biology - 13 Jun 1997

Saha S, Rao D N

Abstract excerpt

The Res subunits of the type III restriction-modification enzymes share a statistically significant amino acid sequence similarity with several RNA and DNA helicases of the so-called DEAD family. It was postulated that in type III restriction enzymes a DNA helicase activity may be required for local unwinding at the cleavage site. The members of this family share seven conserved motifs, all of which are found in...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Conserved Sequence

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Kinetics

Share to Mutagenesis, Site-Directed

Share to Mutation

Share to Phenotype

Source

Identifiers

PMID: 9199404
DOI: 10.1006/jmbi.1997.1045

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations in the Res subunit of the EcoPI restriction enzyme that affect ATP-dependent reactions.PMID 9199404Read ↗

EcoKI with an amino acid substitution in any one of seven DEAD-box motifs has impaired ATPase and endonuclease activities.Semantic proximity Read ↗

The DNA translocation and ATPase activities of restriction-deficient mutants of Eco KI.Semantic proximity Read ↗

Functional consequences of mutating conserved SF2 helicase motifs in the Type III restriction endonuclease EcoP15I translocase domain.Semantic proximity Read ↗

A residue of motif III positions the helicase domains of motor subunit HsdR in restriction-modification enzyme EcoR124I.Semantic proximity Read ↗

Restriction by EcoKI is enhanced by co-operative interactions between target sequences and is dependent on DEAD box motifs.Semantic proximity Read ↗

Structural domains in the type III restriction endonuclease EcoP15I: characterization by limited proteolysis, mass spectrometry and insertional mutagenesis.Semantic proximity Read ↗

Engineering novel restriction endonucleases: principles and applications.Semantic proximity Read ↗

Isolation of a non-classical mutant of the DNA recognition subunit of the type I restriction endonuclease R.EcoR124I.Semantic proximity Read ↗

S-adenosyl-L-methionine is required for DNA cleavage by type III restriction enzymes.Semantic proximity Read ↗

Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme.Semantic proximity Read ↗

S-adenosyl methionine prevents promiscuous DNA cleavage by the EcoP1I type III restriction enzyme.Semantic proximity Read ↗

Characterization of an EcoR124I restriction-modification enzyme produced from a deleted form of the DNA-binding subunit, which results in a novel DNA specificity.Semantic proximity Read ↗

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