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

Solubility engineering of the HhaI methyltransferase.

Protein engineering - 1 Apr 2003

Daujotyte Dalia, Vilkaitis Giedrius, Manelyte Laura, Skalicky Jack, Szyperski Thomas, Klimasauskas Saulius

Abstract excerpt

DNA methylation is involved in epigenetic control of numerous cellular processes in eukaryotes, however, many mechanistic aspects of this phenomenon are not yet understood. A bacterial prototype cytosine-C5 methyltransferase, M.HhaI, serves as a paradigm system for structural and mechanistic studies of biological DNA methylation, but further analysis of the 37 kDa protein is hampered by its insufficient...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Kinetics
Share to Magnetic Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Methylation

Share to Mutagenesis, Site-Directed

Share to Site-Specific DNA-Methyltransferase (Adenine-Specific)

Share to Solubility

Share to Spectrometry, Fluorescence

Source

Identifiers

PMID: 12736373
DOI: 10.1093/proeng/gzg034

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

Solubility engineering of the HhaI methyltransferase.PMID 12736373Read ↗

Investigating the target recognition of DNA cytosine-5 methyltransferase HhaI by library selection using in vitro compartmentalisation.Semantic proximity Read ↗

Non-Histone Protein Methylation: Biological Significance and Bioengineering PotentialSemantic proximity Read ↗

Direct observation of cytosine flipping and covalent catalysis in a DNA methyltransferase.Semantic proximity Read ↗

Engineering the DNA cytosine-5 methyltransferase reaction for sequence-specific labeling of DNA.Semantic proximity Read ↗

Residues distal from the active site that alter enzyme function in M.HhaI DNA cytosine methyltransferase.Semantic proximity Read ↗

HhaI DNA methyltransferase uses the protruding Gln237 for active flipping of its target cytosine.Semantic proximity Read ↗

Altering the sequence specificity of HaeIII methyltransferase by directed evolution using in vitro compartmentalization.Semantic proximity Read ↗

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

Polymorphisms and disease: hotspots of inactivation in methyltransferases.Semantic proximity Read ↗

Identification of amino acids important for target recognition by the DNA:m5C methyltransferase M.NgoPII by alanine-scanning mutagenesis of residues at the protein-DNA interface.Semantic proximity Read ↗

Observing an induced-fit mechanism during sequence-specific DNA methylation.Semantic proximity Read ↗

Substrate specificity of human protein arginine methyltransferase 7 (PRMT7): the importance of acidic residues in the double E loop.Semantic proximity Read ↗

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