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

A novel DNA binding and nuclease activity in domain III of Mu transposase: evidence for a catalytic region involved in donor cleavage.

The EMBO journal - 1 Aug 1995

Wu Z, Chaconas G

Abstract excerpt

The Mu A protein is a 75 kDa transposase organized into three structural domains. By severing the C-terminal region (domain III) from the remainder of the protein, we unmasked a novel non-specific DNA binding and nuclease activity in this region. Deletion analysis localized both activities to a 26 amino acid stretch (aa 575-600) which remarkably remained active in DNA binding and cleavage. The two activities were...

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 Base Sequence
Share to Binding Sites

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

Share to DNA-Binding Proteins

Share to DNA, Viral

Share to Molecular Sequence Data

Share to Mutation

Share to Sequence Deletion

Source

Open in PubMed Open full text

Identifiers

PMID: 7641701
DOI: 10.1002/j.1460-2075.1995.tb00053.x
PMCID: PMC394458

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

A novel DNA binding and nuclease activity in domain III of Mu transposase: evidence for a catalytic region involved in donor cleavage.PMID 7641701Read ↗

Mutations in domain III alpha of the Mu transposase: evidence suggesting an active site component which interacts with the Mu-host junction.Semantic proximity Read ↗

Step-arrest mutants of phage Mu transposase. Implications in DNA-protein assembly, Mu end cleavage, and strand transfer.Semantic proximity Read ↗

Tn5 transposase active site mutants.Semantic proximity Read ↗

Defining functional regions of the IS903 transposase.Semantic proximity Read ↗

Two mutations of phage mu transposase that affect strand transfer or interactions with B protein lie in distinct polypeptide domains.Semantic proximity Read ↗

A bifunctional DNA binding region in Tn5 transposase.Semantic proximity Read ↗

Mu transpososome activity-profiling yields hyperactive MuA variants for highly efficient genetic and genome engineering.Semantic proximity Read ↗

Complete transposition requires four active monomers in the mu transposase tetramer.Semantic proximity Read ↗

Sequence and positional requirements for DNA sites in a mu transpososome.Semantic proximity Read ↗

Crosstalk between transposase subunits during cleavage of the mariner transposon.Semantic proximity Read ↗

MuA transposase separates DNA sequence recognition from catalysis.Semantic proximity Read ↗

Effect of mutations in the Mu-host junction region on transpososome assembly.Semantic proximity Read ↗

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