Evidence map›Paper›PMID 27899559›Full record

ArticleNucleic acids research2017

Division of labor among Mycobacterium smegmatis RNase H enzymes: RNase H1 activity of RnhA or RnhC is essential for growth whereas RnhB and RnhA guard against killing by hydrogen peroxide in stationary phase.

Richa Gupta, Debashree Chatterjee, Michael S Glickman, Stewart Shuman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
11.7field-weighted citation impact, top 1% 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

15 citing papers in PubMed, 113 citations in OpenAlex.

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  10. Cells · 2021
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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

4 authors at 1 institution in 1 country.

Richa GuptaImmunology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Debashree ChatterjeeMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Michael S GlickmanImmunology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA glickmam@mskcc.org.
Stewart ShumanMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA s-shuman@ski.mskcc.org.
Memorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
Novel pathway of DNA inter-strand crosslink repair in mycobacteriaR01AI064693 · NIAID · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Michael S Glickman, Stewart H Shuman · 2005 to 2026
$11.1M
NCI NIH HHS P30 CA008748NIAID NIH HHS R01 AI064693
6 · The paper itself

Abstract

RNase H enzymes sense the presence of ribonucleotides in the genome and initiate their removal by incising the ribonucleotide-containing strand of an RNA:DNA hybrid. Mycobacterium smegmatis encodes four RNase H enzymes: RnhA, RnhB, RnhC and RnhD. Here, we interrogate the biochemical activity and nucleic acid substrate specificity of RnhA. We report that RnhA (like RnhC characterized previously) is an RNase H1-type magnesium-dependent endonuclease with stringent specificity for RNA:DNA hybrid duplexes. Whereas RnhA does not incise an embedded mono-ribonucleotide, it can efficiently cleave within tracts of four or more ribonucleotides in duplex DNA. We gained genetic insights to the division of labor among mycobacterial RNases H by deleting the rnhA, rnhB, rnhC and rnhD genes, individually and in various combinations. The salient conclusions are that: (i) RNase H1 activity is essential for mycobacterial growth and can be provided by either RnhC or RnhA; (ii) the RNase H2 enzymes RnhB and RnhD are dispensable for growth and (iii) RnhB and RnhA collaborate to protect M. smegmatis against oxidative damage in stationary phase. Our findings highlight RnhC, the sole RNase H1 in pathogenic mycobacteria, as a candidate drug discovery target for tuberculosis and leprosy.

Indexed as

Gene Expression Regulation, BacterialGenome, BacterialAmino Acid SequenceBacterial ProteinsBase SequenceCloning, MolecularDNA, BacterialEscherichia coliHydrogen PeroxideIsoenzymesMycobacterium smegmatisRecombinant ProteinsRibonuclease HRibonucleotidesRNA, BacterialSequence AlignmentBacterial ProteinsDNA, BacterialHydrogen PeroxideIsoenzymesRecombinant ProteinsRibonuclease Hribonuclease HIRibonucleotidesRNA, Bacterial

Identifiers

PMID27899559
PMCPMC5224475
OpenAlexW2557733467

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.