Evidence map›Paper›PMID 19638340›Full record

ArticleThe Journal of biological chemistry2009

Bacillus subtilis trp Leader RNA: RNase J1 endonuclease cleavage specificity and PNPase processing.

Gintaras Deikus, David H Bechhofer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. In vivo 3'-to-5' exoribonuclease targetomes ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  4. Article
  5. Article
  6. Initiation of mRNA decay in bacteria.Cellular and molecular life sciences : CMLS · 2014
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. RNAs: regulators of bacterial virulence.Nature reviews. Microbiology · 2010
    Review
  12. Article
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.

Gintaras DeikusDepartment of Pharmacology and Systems Therapeutics, Mount Sinai School of Medicine of New York University, New York, New York 10029-6574, USA.
David H Bechhofer
Icahn School of Medicine at Mount Sinai · US

Funding

INITIATION OF MRNA DECAY IN BACILLUS SUBTILISR01GM048804 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI BECHHOFER, DAVID H · 1993 to 2010
$2.9M
NIGMS NIH HHS GM48804NIGMS NIH HHS R01 GM048804
6 · The paper itself

Abstract

In the presence of ample tryptophan, transcription from the Bacillus subtilis trp operon promoter terminates to give a 140-nucleotide trp leader RNA. Turnover of trp leader RNA has been shown to depend on RNase J1 cleavage at a single-stranded, AU-rich region just upstream of the 3' transcription terminator. The small size of trp leader RNA and its strong dependence on RNase J1 cleavage for decay make it a suitable substrate for analyzing the requirements for RNase J1 target site specificity. trp leader RNAs with nucleotide changes around the RNase J1 target site were more stable than wild-type trp leader RNA, showing that sequences on either side of the cleavage site contribute to RNase J1 recognition. An analysis of decay intermediates from these mutants suggested limited 3'-to-5' exonuclease processing from the native 3' end. trp leader RNAs were designed that contained wild-type or mutant RNase J1 targets elsewhere on the molecule. The presence of an additional RNase J1 cleavage site resulted in faster RNA decay, depending on its location. Addition of a 5' tail containing 7 A residues caused destabilization of trp leader RNAs. Surprisingly, addition at the 5' end of a strong stem loop structure that is known to stabilize other RNAs did not result in a longer trp leader RNA half-life, suggesting that the RNase J1 cleavage site may be accessed directly. In the course of these experiments, we found evidence that polynucleotide phosphorylase processivity was inhibited by a GCGGCCGC sequence.

Indexed as

Bacillus subtilisBacterial ProteinsBase SequenceBinding SitesBlotting, NorthernEndoribonucleasesMolecular Sequence DataMutationNucleic Acid ConformationOperonPolyribonucleotide NucleotidyltransferaseRNA, BacterialRNA-Binding ProteinsRNA StabilitySequence Homology, Nucleic AcidSubstrate SpecificityBacterial ProteinsEndoribonucleasesMtrB protein, BacteriaPolyribonucleotide NucleotidyltransferaseRNA, BacterialRNA-Binding ProteinsTranscription FactorsTryptophan

Identifiers

PMID19638340
PMCPMC2785327
OpenAlexW2008416050

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.