Evidence map›Paper›PMID 41196441›Full record

ReviewMolecular biology reports2025

HemK class methyltransferase, a protein translation regulator: role in growth, development and phenotypic diversity.

Swapnaneel Pal, Surjit Singh

Abstract readReview
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In one paragraph

Review in Molecular biology reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Swapnaneel PalDepartment of Biotechnology, School of Health Sciences & Translational Research, Sister Nivedita University, New Town, 700156, West Bengal, India.
Surjit SinghDepartment of Biotechnology, School of Health Sciences & Translational Research, Sister Nivedita University, New Town, 700156, West Bengal, India. surjit.s@snuniv.ac.in.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Across eukaryotic and prokaryotic life forms, translation termination occurs followed by disassembly of ribosomal subunits and release of the nascent polypeptide. This process is governed by the presence of Release factors or translation termination factors, which render polypeptide hydrolysis from the peptidyl t-RNA by interacting with its conserved GGQ motif. Studies have shown that methylation of Release Factors by Methyltransferases at this highly conserved motif is necessary for efficient translation termination; failure to do so leads to the accumulation of polyribosomes and subsequently altered protein synthesis, ultimately resulting in an undesired phenotype. HemK class methyltransferases are a widely conserved class of enzymes involved in the methylation of Glutamine. Due to methylation of release factors by HemK at the GGQ motif, faithful translation termination occurs. Its absence leads to reduced stress tolerance as well as developmental abnormalities and other detrimental effects. Studies have suggested HemK to be associated with DNA methylation as well as chromatin remodelling activities. This review provides a brief overview of the role of HemK as a translational as well as transcriptional regulator, and its function in prokaryotic and eukaryotic systems.

Indexed as

MethyltransferasesProtein BiosynthesisAnimalsDNA MethylationHumansPeptide Chain Termination, TranslationalPeptide Termination FactorsPhenotypeMethyltransferasesPeptide Termination FactorsGrowth and developmentHemKMethyltransferaseProtein translationRibosomal release factor

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.