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

Specific DNA Recognition by EcoRV Restriction Endonuclease Induced by Calcium Ions

1 Jan 1995

Abstract excerpt

In the presence of Mg2+, the EcoRV restriction endonuclease cleaves DNA specifically at its recognition sequence, but in the absence of divalent metal ions, it binds DNA without any specificity: gel-shift experiments had revealed multiple EcoRV-DNA complexes, due to the binding of one, two, three, or more molecules of protein per molecule of DNA, with the same equilibrium constant for each association. In this...

Read the complete abstract on PubMed

Topics

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

Share to Viral Infections and Immunology Research
Share to Viral Infectious Diseases and Gene Expression in Insects
Share to Virus-based gene therapy research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 7827059
DOI: 10.1021/bi00004a002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Specific DNA Recognition by EcoRV Restriction Endonuclease Induced by Calcium IonsPMID 7827059Read ↗

Catalytic efficiency and sequence selectivity of a restriction endonuclease modulated by a distal manganese ion binding site.Semantic proximity Read ↗

Positively charged C-terminal subdomains of EcoRV endonuclease: contributions to DNA binding, bending, and cleavage.Semantic proximity Read ↗

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

Dual role for Zn2+ in maintaining structural integrity and inducing DNA sequence specificity in a promiscuous endonuclease.Semantic proximity Read ↗

Determination of the DNA bend angle induced by the restriction endonuclease EcoRV in the presence of Mg2+.Semantic proximity Read ↗

DNA cleavage by EcoRV endonuclease: two metal ions in three metal ion binding sites.Semantic proximity Read ↗

Increasing cleavage specificity and activity of restriction endonuclease KpnI.Semantic proximity Read ↗

Transcription regulation of the EcoRV restriction-modification systemSemantic proximity Read ↗

Identification and mutational analysis of Mg2+ binding site in EcoP15I DNA methyltransferase: involvement in target base eversion.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 ↗

MnlI--The member of H-N-H subtype of Type IIS restriction endonucleases.Semantic proximity Read ↗

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

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