Evidence map›Paper›PMID 20007328›Full record

ArticleRNA (New York, N.Y.)2010

Bacterial Hen1 is a 3' terminal RNA ribose 2'-O-methyltransferase component of a bacterial RNA repair cassette.

Ruchi Jain, Stewart Shuman

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
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

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.

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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. HENMT1: an RNA methyltransferase in biology and disease.Journal of Zhejiang University. Science. B · 2026
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  16. Molecular basis of bacterial protein Hen1 activating the ligase activity of bacterial protein Pnkp for RNA repair.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  17. Review
  18. The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family.Proceedings of the National Academy of Sciences of the United States of America · 2012
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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 at 1 institution in 1 country.

Ruchi JainMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA.
Stewart Shuman
Kettering University · US

Funding

Viral RNA Modifying EnzymesR01GM042498 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SHUMAN, STEWART H · 1989 to 2017
$6.8M
NIGMS NIH HHS GM42498NIGMS NIH HHS R01 GM042498
6 · The paper itself

Abstract

Hen1 is an RNA ribose 2'-O-methyltransferase that modifies the 3' terminal nucleoside of eukaryal small regulatory RNAs. Here, we report that Hen1 homologs are present in bacterial proteomes from eight different phyla. Bacterial Hen1 is encoded by the proximal ORF of a two-gene operon that also encodes polynucleotide kinase-phosphatase (Pnkp), an RNA repair enzyme. Purified recombinant Clostridium thermocellum Hen1 is a homodimer of a 465-amino acid polypeptide. CthHen1 catalyzes methyl transfer from AdoMet to the 3' terminal nucleoside of an RNA oligonucleotide, but is unreactive with a synonymous DNA oligonucleotide or an RNA with a single 3'-terminal deoxyribose sugar. CthHen1 is optimally active at alkaline pH and dependent on manganese. Activity is inhibited by AdoHcy and abolished by mutations D291A and D316A in the putative AdoMet-binding pocket. The C-terminal fragment, Hen1-(259-465), comprises an autonomous monomeric methyltransferase domain.

Indexed as

Acetivibrio thermocellusAmino Acid SequenceBacterial ProteinsBase SequenceMethyltransferasesMolecular Sequence DataProtein MultimerizationProtein Structure, TertiaryRecombinant ProteinsRNA, BacterialS-AdenosylmethionineSequence Homology, Amino AcidSubstrate SpecificityBacterial ProteinsMethyltransferasesRecombinant ProteinsRNA 2'-O-methyltransferaseRNA, BacterialS-Adenosylmethionine

Identifiers

PMID20007328
PMCPMC2811661
OpenAlexW2160784870

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.