ArticleNucleic acids research2009
A directed evolution design of a GCG-specific DNA hemimethylase.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- From sequence to activity: the HgaI-homologous restriction modification system RM.MhoVI of Mycoplasma hominis.BMC microbiology · 2025Article
- Conversion of the CG specific M.MpeI DNA methyltransferase into an enzyme predominantly methylating CCA and CCC sites.Nucleic acids research · 2024Article
- Revealing Drivers for Carboxy-ACS chemical biology · 2023Article
- Selective chemical tracking of Dnmt1 catalytic activity in live cells.Molecular cell · 2022Article
- DNA Labeling Using DNA Methyltransferases.Advances in experimental medicine and biology · 2022Article
- Methyltransferase-Directed Labeling of Biomolecules and its Applications.Angewandte Chemie (International ed. in English) · 2017Review
- DNA Labeling Using DNA Methyltransferases.Advances in experimental medicine and biology · 2016Review
- Metadynamics simulation study on the conformational transformation of HhaI methyltransferase: an induced-fit base-flipping hypothesis.BioMed research international · 2014Article
- Article
- Engineering the DNA cytosine-5 methyltransferase reaction for sequence-specific labeling of DNA.Nucleic acids research · 2012Article
- A yeast one-hybrid system to screen for methylated DNA-binding proteins.Nucleic acids research · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
DNA cytosine-5 methyltransferases (C5-MTases) are valuable models to study sequence-specific modification of DNA and are becoming increasingly important tools for biotechnology. Here we describe a structure-guided rational protein design combined with random mutagenesis and selection to change the specificity of the HhaI C5-MTase from GCGC to GCG. The specificity change was brought about by a five-residue deletion and introduction of two arginine residues within and nearby one of the target recognizing loops. DNA protection assays, bisulfite sequencing and enzyme kinetics showed that the best selected variant is comparable to wild-type M.HhaI in terms of sequence fidelity and methylation efficiency, and supersedes the parent enzyme in transalkylation of DNA using synthetic cofactor analogs. The designed C5-MTase can be used to produce hemimethylated CpG sites in DNA, which are valuable substrates for studies of mammalian maintenance MTases.
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Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.