Evidence map›Paper›PMID 22439849›Full record

ArticleBiochemistry2012

Interaction of the histone mRNA hairpin with stem-loop binding protein (SLBP) and regulation of the SLBP-RNA complex by phosphorylation and proline isomerization.

Minyou Zhang, TuKiet T Lam, Marco Tonelli, William F Marzluff, Roopa Thapar

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

29 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Replication-dependent histone biosynthesis is coupled to cell-cycle commitment.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. RNA architecture influences plant biology.Journal of experimental botany · 2021
    Review
  7. Article
  8. Discovery and Validation of Circulating Biomarkers of Colorectal Adenoma by High-Depth Small RNA Sequencing.Clinical cancer research : an official journal of the American Association for Cancer Research · 2018
    Article
  9. BEAM web server: a tool for structural RNA motif discovery.Bioinformatics (Oxford, England) · 2018
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Molecular mechanisms for the regulation of histone mRNA stem-loop-binding protein by phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

5 authors at 4 institutions in 1 country.

Minyou ZhangHauptman-Woodward Medical Research Institute, Buffalo, New York 14203, United States.
TuKiet T Lam
Marco Tonelli
William F Marzluff
Roopa Thapar
Hauptman-Woodward Medical Research Institute · USUniversity of North Carolina at Chapel Hill · USUniversity of Wisconsin–Madison · USW. M. Keck Foundation · US

Funding

WATER DISTRIB:PHYSICAL PROPERT:PIZZA &LMPS MOZZARELLA CHEESES:EARLY STAGE MATURP41RR002301 · NCRR · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN LUTE · 1985 to 2011
$13.0M
900 MHz NMR Spectrometer Biomolecular InvestigationsP41GM066326 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI MARKLEY, JOHN L · 2002 to 2006
$5.0M
Phosphorylation dependent recognition of a histone mRNA hairpin by SLBPR01GM076660 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MARZLUFF, WILLIAM F. · 2006 to 2009
$1.1M
WIDE-BORE 9.4 TESLA NMR SPECTROMETER FOR UW-MADISONS10RR002781 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1986 to 1986
–
CONSOLE UPGRADES FOR NMR FACILITYS10RR008438 · NCRR · UNIVERSITY OF WISCONSIN MADISON · PI MARKLEY, JOHN L · 1993 to 1993
–
NCRR NIH HHS P41 RR002301NCRR NIH HHS P41RR02301NCRR NIH HHS S10 RR002781NCRR NIH HHS S10 RR008438NIGMS NIH HHS 1R01-GM076660NIGMS NIH HHS 1R01-GM076660-04S1NIGMS NIH HHS P41 GM066326NIGMS NIH HHS P41GM66326NIGMS NIH HHS R01 GM076660
6 · The paper itself

Abstract

In metazoans, the majority of histone proteins are generated from replication-dependent histone mRNAs. These mRNAs are unique in that they are not polyadenylated but have a stem-loop structure in their 3' untranslated region. An early event in 3' end formation of histone mRNAs is the binding of stem-loop binding protein (SLBP) to the stem-loop structure. Here we provide insight into the mechanism by which SLBP contacts the histone mRNA. There are two binding sites in the SLBP RNA binding domain for the histone mRNA hairpin. The first binding site (Glu129-Val158) consists of a helix-turn-helix motif that likely recognizes the unpaired uridines in the loop of the histone hairpin and, upon binding, destabilizes the first G-C base pair at the base of the stem. The second binding site lies between residues Arg180 and Pro200, which appears to recognize the second G-C base pair from the base of the stem and possibly regions flanking the stem-loop structure. We show that the SLBP-histone mRNA complex is regulated by threonine phosphorylation and proline isomerization in a conserved TPNK sequence that lies between the two binding sites. Threonine phosphorylation increases the affinity of SLBP for histone mRNA by slowing the off rate for complex dissociation, whereas the adjacent proline acts as a critical hinge that may orient the second binding site for formation of a stable SLBP-histone mRNA complex. The nuclear magnetic resonance and kinetic studies presented here provide a framework for understanding how SLBP recognizes histone mRNA and highlight possible structural roles of phosphorylation and proline isomerization in RNA binding proteins in remodeling ribonucleoprotein complexes.

Indexed as

Amino Acid SequenceAnimalsBinding SitesDrosophila ProteinsHistonesHumansKineticsMolecular Sequence DatamRNA Cleavage and Polyadenylation FactorsNuclear ProteinsNucleic Acid ConformationPhosphorylationProlineRNA-Binding ProteinsRNA, MessengerDrosophila ProteinsHistonesmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsProlineRNA-Binding ProteinsRNA, MessengerSLBP protein, DrosophilaSLBP protein, human

Identifiers

PMID22439849
PMCPMC3328597
OpenAlexW2094204895

What OpenQuestion holds

Textmetadata
LicenceTDM
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.