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

Genetic analysis of the base-specific contacts of BamHI restriction endonuclease.

Journal of molecular biology - 29 Jan 1999

Dorner L F, Bitinaite J, Whitaker R D, Schildkraut I

Abstract excerpt

Here, we investigate the highly specific interaction of the BamHI endonuclease with its cognate recognition sequence GGATCC by determining which amino acid residues can be substituted at the DNA interface while maintaining specificity. Mutational studies, together with the structural determination of the restriction endonuclease BamHI have revealed the amino acid residues which are involved in DNA catalysis and...

Read the complete abstract on PubMed

Topics

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

Share to Protein Conformation
Share to Amino Acid Sequence
Share to Base Sequence

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

Share to Binding Sites

Share to DNA, Bacterial

Share to Escherichia coli

Share to Molecular Sequence Data

Share to Mutation

Source

Identifiers

PMID: 9917393
DOI: 10.1006/jmbi.1998.2408

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

Genetic analysis of the base-specific contacts of BamHI restriction endonuclease.PMID 9917393Read ↗

A mutant of BamHI restriction endonuclease which requires N6-methyladenine for cleavage.Semantic proximity Read ↗

Protecting recognition sequences on DNA by a cleavage-deficient restriction endonuclease.Semantic proximity Read ↗

Isolation of BsoBI restriction endonuclease variants with altered substrate specificity.Semantic proximity Read ↗

The BsaHI restriction-modification system: cloning, sequencing and analysis of conserved motifs.Semantic proximity Read ↗

Changing the target base specificity of the EcoRV DNA methyltransferase by rational de novo protein-design.Semantic proximity Read ↗

Structural mechanisms of the degenerate sequence recognition by Bse634I restriction endonuclease.Semantic proximity Read ↗

Analyzing the functional organization of a novel restriction modification system, the BcgI system.Semantic proximity Read ↗

Implications for switching restriction enzyme specificities from the structure of BstYI bound to a BglII DNA sequence.Semantic proximity Read ↗

Engineering of restriction endonucleases: using methylation activity of the bifunctional endonuclease Eco57I to select the mutant with a novel sequence specificity.Semantic proximity Read ↗

Combinatorial mutagenesis of three major groove-contacting residues of EcoRI: single and double amino acid replacements retaining methyltransferase-sensitive activities.Semantic proximity Read ↗

Role of DNA minor groove interactions in substrate recognition by the M.SinI and M.EcoRII DNA (cytosine-5) methyltransferases.Semantic proximity Read ↗

Towards the design of rare cutting restriction endonucleases: using directed evolution to generate variants of EcoRV differing in their substrate specificity by two orders of magnitude.Semantic proximity Read ↗

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