Evidence map›Paper›PMID 17717080›Full record

ArticleRNA (New York, N.Y.)2007

Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAs.

Anna Perederina, Olga Esakova, Hasan Koc, Mark E Schmitt, Andrey S Krasilnikov

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.3field-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

32 citing papers in PubMed, 49 citations in OpenAlex.

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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

5 authors at 2 institutions in 1 country.

Anna PerederinaDepartment of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
Olga Esakova
Hasan Koc
Mark E Schmitt
Andrey S Krasilnikov
Pennsylvania State University · USSUNY Upstate Medical University · US

Funding

Control of the cell cycle by mRNA degradation.R01GM063798 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI SCHMITT, MARK E · 2003 to 2011
$2.3M
NIGMS NIH HHS GM063798NIGMS NIH HHS R01 GM063798
6 · The paper itself

Abstract

Pop6 and Pop7 are protein subunits of Saccharomyces cerevisiae RNase MRP and RNase P. Here we show that bacterially expressed Pop6 and Pop7 form a soluble heterodimer that binds the RNA components of both RNase MRP and RNase P. Footprint analysis of the interaction between the Pop6/7 heterodimer and the RNase MRP RNA, combined with gel mobility assays, demonstrates that the Pop6/7 complex binds to a conserved region of the P3 domain. Binding of these proteins to the MRP RNA leads to local rearrangement in the structure of the P3 loop and suggests that direct interaction of the Pop6/7 complex with the P3 domain of the RNA components of RNases MRP and P may mediate binding of other protein components. These results suggest a role for a key element in the RNase MRP and RNase P RNAs in protein binding, and demonstrate the feasibility of directly studying RNA-protein interactions in the eukaryotic RNases MRP and P complexes.

Indexed as

Base SequenceDimerizationEndoribonucleasesMolecular Sequence DataNucleic Acid ConformationProtein Structure, TertiaryProtein SubunitsRibonuclease PRNA, FungalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsEndoribonucleasesmitochondrial RNA-processing endoribonucleaseProtein SubunitsRibonuclease PRNA, FungalSaccharomyces cerevisiae Proteins

Identifiers

PMID17717080
PMCPMC1986809
OpenAlexW2054537008

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.