Evidence map›Paper›PMID 29403013›Full record

ArticleNature microbiology2018

The host-encoded RNase E endonuclease as the crRNA maturation enzyme in a CRISPR-Cas subtype III-Bv system.

Juliane Behler, Kundan Sharma, Viktoria Reimann, Annegret Wilde, Henning Urlaub, Wolfgang R Hess

Abstract read
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In one paragraph

Article in Nature microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

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

46 citing papers in PubMed.

  1. From pond to platform: howJournal of bacteriology · 2026
    Review
  2. Archaeal RNA processing and regulation: expanding the functional landscape.Microbiology and molecular biology reviews : MMBR · 2025
    Review
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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

6 authors.

Juliane BehlerGenetics and Experimental Bioinformatics, Faculty of Biology, University of Freiburg, Freiburg, Germany.
Kundan SharmaBioanalytics Research Group, Department of Clinical Chemistry, University Medical Centre, Göttingen, Germany.
Viktoria ReimannGenetics and Experimental Bioinformatics, Faculty of Biology, University of Freiburg, Freiburg, Germany.
Annegret WildeMolecular Genetics, Faculty of Biology, University of Freiburg, Freiburg, Germany.ORCID http://orcid.org/0000-0003-0935-8415
Henning UrlaubBioanalytics Research Group, Department of Clinical Chemistry, University Medical Centre, Göttingen, Germany.
Wolfgang R HessGenetics and Experimental Bioinformatics, Faculty of Biology, University of Freiburg, Freiburg, Germany. wolfgang.hess@biologie.uni-freiburg.de.ORCID http://orcid.org/0000-0002-5340-3423

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specialized RNA endonucleases for the maturation of clustered regularly interspaced short palindromic repeat (CRISPR)-derived RNAs (crRNAs) are critical in CRISPR-CRISPR-associated protein (Cas) defence mechanisms. The Cas6 and Cas5d enzymes are the RNA endonucleases in many class 1 CRISPR-Cas systems. In some class 2 systems, maturation and effector functions are combined within a single enzyme or maturation proceeds through the combined actions of RNase III and trans-activating CRISPR RNAs (tracrRNAs). Three separate CRISPR-Cas systems exist in the cyanobacterium Synechocystis sp. PCC 6803. Whereas Cas6-type enzymes act in two of these systems, the third, which is classified as subtype III-B variant (III-Bv), lacks cas6 homologues. Instead, the maturation of crRNAs proceeds through the activity of endoribonuclease E, leaving unusual 13- and 14-nucleotide-long 5'-handles. Overexpression of RNase E leads to overaccumulation and knock-down to the reduced accumulation of crRNAs in vivo, suggesting that RNase E is the limiting factor for CRISPR complex formation. Recognition by RNase E depends on a stem-loop in the CRISPR repeat, whereas base substitutions at the cleavage site trigger the appearance of secondary products, consistent with a two-step recognition and cleavage mechanism. These results suggest the adaptation of an otherwise very conserved housekeeping enzyme to accommodate new substrates and illuminate the impressive plasticity of CRISPR-Cas systems that enables them to function in particular genomic environments.

Indexed as

CRISPR-Cas SystemsClustered Regularly Interspaced Short Palindromic RepeatsEndoribonucleasesRNARNA CleavageSubstrate SpecificitySynechocystisEndoribonucleasesribonuclease ERNA

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.