Evidence map›Paper›PMID 22355167›Full record

ArticleRNA (New York, N.Y.)2012

YbxF and YlxQ are bacterial homologs of L7Ae and bind K-turns but not K-loops.

Nathan J Baird, Jinwei Zhang, Tomoko Hamma, Adrian R Ferré-D'Amaré

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

40 citing papers in PubMed, 59 citations in OpenAlex.

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  12. Improving RNA Crystal Diffraction Quality by Postcrystallization Treatment.Methods in molecular biology (Clifton, N.J.) · 2021
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  18. Crystal structures of the archaeal RNase P protein Rpp38 in complex with RNA fragments containing a K-turn motif.Acta crystallographica. Section F, Structural biology communications · 2018
    Article
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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 2 institutions in 1 country.

Nathan J BairdLaboratory of RNA Biophysics and Cellular Physiology, National Heart, Lung and Blood Institute, Bethesda, Maryland 20892-8012, USA.
Jinwei Zhang
Tomoko Hamma
Adrian R Ferré-D'Amaré
National Heart Lung and Blood Institute · USPacific Northwest University of Health Sciences · US

Funding

RNA: Structure, Biophysics and PhysiologyZIAHL006102 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FERRÉ-D'AMARÉ, ADRIAN · 2011 to 2025
$14.6M
Protein Analysis FacilityZICHL006028 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI LEE, DUCK-YEON · 2009 to 2014
$1.5M
Intramural NIH HHS
6 · The paper itself

Abstract

The archaeal protein L7Ae and eukaryotic homologs such as L30e and 15.5kD comprise the best characterized family of K-turn-binding proteins. K-turns are an RNA motif comprised of a bulge flanked by canonical and noncanonical helices. They are widespread in cellular RNAs, including bacterial gene-regulatory RNAs such as the c-di-GMP-II, lysine, and SAM-I riboswitches, and the T-box. The existence in bacteria of K-turn-binding proteins of the L7Ae family has not been proven, although two hypothetical proteins, YbxF and YlxQ, have been proposed to be L7Ae homologs based on sequence conservation. Using purified, recombinant proteins, we show that Bacillus subtilis YbxF and YlxQ bind K-turns (K(d) ~270 nM and ~2300 nM, respectively). Crystallographic structure determination demonstrates that both YbxF and YlxQ adopt the same overall fold as L7Ae. Unlike the latter, neither bacterial protein recognizes K-loops, a structural motif that lacks the canonical helix of the K-turn. This property is shared between the bacterial and eukaryal family members. Comparison of our structure of YbxF in complex with the K-turn of the SAM-I riboswitch and previously determined structures of archaeal and eukaryal homologs bound to RNA indicates that L7Ae approaches the K-turn at a unique angle, which results in a considerably larger RNA-protein interface dominated by interactions with the noncanonical helix of the K-turn. Thus, the inability of the bacterial and eukaryal L7Ae homologs to bind K-loops probably results from their reliance on interactions with the canonical helix. The biological functions of YbxF and YlxQ remain to be determined.

Indexed as

Amino Acid SequenceBacillus subtilisBacterial ProteinsCrystallography, X-RayMolecular Sequence DataProtein BindingSequence Homology, Amino AcidBacterial Proteins

Identifiers

PMID22355167
PMCPMC3312563
OpenAlexW2162528693

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.