Evidence map›Paper›PMID 25787880›Full record

ArticleJournal of applied genetics2015

Relaxed specificity of prokaryotic DNA methyltransferases results in DNA site-specific modification of RNA/DNA heteroduplexes.

Ewa Wons, Iwona Mruk, Tadeusz Kaczorowski

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Article in Journal of applied genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
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1 · What the graph read from it

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.

2 · The registry

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Ewa WonsDepartment of Microbiology, University of Gdansk, Wita Stwosza 59, 80-308, Gdansk, Poland.
Iwona MrukDepartment of Microbiology, University of Gdansk, Wita Stwosza 59, 80-308, Gdansk, Poland.
Tadeusz KaczorowskiDepartment of Microbiology, University of Gdansk, Wita Stwosza 59, 80-308, Gdansk, Poland. tadeusz.kaczorowski@biol.ug.edu.pl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RNA/DNA hybrid duplexes regularly occur in nature, for example in transcriptional R loops. Their susceptibility to modification by DNA-specific or RNA-specific enzymes is, thus, a biologically relevant question, which, in addition, has possible biotechnological implications. In this study, we investigated the activity of four isospecific DNA methyltransferases (M.EcoVIII, M.LlaCI, M.HindIII, M.BstZ1II) toward an RNA/DNA duplex carrying one 5'-AAGCUU-3'/3'-TTCGAA-5' target sequence. The analyzed enzymes belong to the β-group of adenine N6-methyltransferases and recognize the palindromic DNA sequence 5'-AAGCTT-3'/3'-TTCGAA-5'. Under standard conditions, none of these isospecific enzymes could detectibly methylate the RNA/DNA duplex. However, the addition of agents that generally relax specificity, such as dimethyl sulfoxide (DMSO) and glycerol, resulted in substantial methylation of the RNA/DNA duplex by M.EcoVIII and M.LlaCI. Only the DNA strand of the RNA/DNA duplex was methylated. The same was not observed for M.HindIII or M.BstZ1II. This is, to our knowledge, the first report that demonstrates such activity by prokaryotic DNA methyltransferases. Possible applications of these findings in a laboratory practice are also discussed.

Indexed as

BacteriaBacterial ProteinsDNADNA Modification MethylasesNucleic Acid HeteroduplexesRNASubstrate SpecificityBacterial ProteinsDNADNA Modification MethylasesNucleic Acid HeteroduplexesRNAProkaryotic DNA methyltransferaseRelaxed specificityRNA/DNA hybrid

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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.