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

Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I.

Journal of molecular biology - 23 Feb 2001

Janscak P, Sandmeier U, Szczelkun M D, Bickle T A

Abstract excerpt

DNA cleavage by type III restriction endonucleases requires two inversely oriented asymmetric recognition sequences and results from ATP-dependent DNA translocation and collision of two enzyme molecules. Here, we characterized the structure and mode of action of the related EcoP1I and EcoP15I enzymes. Analytical ultracentrifugation and gel quantification revealed a common Res(2)Mod(2) subunit stoichiometry....

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

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA, Superhelical

Share to Protein Structure, Quaternary

Share to Protein Subunits

Share to Sequence Alignment

Share to Substrate Specificity

Share to Ultracentrifugation

Source

Identifiers

PMID: 11178902
DOI: 10.1006/jmbi.2000.4411

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

Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I.PMID 11178902Read ↗

Single-site DNA cleavage by Type III restriction endonuclease requires a site-bound enzyme and a trans-acting enzyme that are ATPase-activated.Semantic proximity Read ↗

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

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

Asymmetric DNA methylation by dimeric EcoP15I DNA methyltransferase.Semantic proximity Read ↗

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

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

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

Engineering of variants of the restriction endonuclease EcoRV that depend in their cleavage activity on the flexibility of sequences flanking the recognition site.Semantic proximity Read ↗

DNA-mediated coupling of ATPase, translocase and nuclease activities of a Type ISP restriction-modification enzyme.Semantic proximity Read ↗

Structural insights into assembly, operation and inhibition of a type I restriction-modification system.Semantic proximity Read ↗

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

The DNA recognition subunit of the type IB restriction-modification enzyme EcoAI tolerates circular permutions of its polypeptide chain.Semantic proximity Read ↗

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