Evidence map›Paper›PMID 12242288›Full record

ArticleMolecular and cellular biology2002

The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro.

Ricardo Sànchez, William F Marzluff

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

77 citing papers in PubMed, 133 citations in OpenAlex.

  1. SLBP-independent control of maternal histone mRNA.bioRxiv : the preprint server for biology · 2026
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  10. Polyadenylation of canonical histone H3.1 in carcinogenesis.Advances in pharmacology (San Diego, Calif.) · 2023
    Article
  11. Dual Leucine Zipper Kinase Regulates Dscam Expression through a Noncanonical Function of the Cytoplasmic Poly(A)-Binding Protein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
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17 more citing papers are in PubMed but not listed here.

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 2 countries.

Ricardo SànchezProgram in Molecular Biology and Biotechnology, Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
William F Marzluff
University of North Carolina at Chapel Hill · US

Funding

HISTONE MRNA REGULATION IN DEVELOPMENTR01GM058921 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DURONIO, ROBERT J, MARZLUFF, WILLIAM F. · 1999 to 2025
$11.6M
NIGMS NIH HHS GM58921NIGMS NIH HHS R01 GM058921
6 · The paper itself

Abstract

Metazoan replication-dependent histone mRNAs end in a conserved stem-loop rather than in the poly(A) tail found on all other mRNAs. The 3' end of histone mRNA binds a single class of proteins, the stem-loop binding proteins (SLBP). In Xenopus, there are two SLBPs: xSLBP1, the homologue of the mammalian SLBP, which is required for processing of histone pre-mRNA, and xSLBP2, which is expressed only during oogenesis and is bound to the stored histone mRNA in Xenopus oocytes. The stem-loop is required for efficient translation of histone mRNAs and substitutes for the poly(A) tail, which is required for efficient translation of other eucaryotic mRNAs. When a rabbit reticulocyte lysate is programmed with uncapped luciferase mRNA ending in the histone stem-loop, there is a three- to sixfold increase in translation in the presence of xSLBP1 while xSLBP2 has no effect on translation. Neither SLBP affected the translation of a luciferase mRNA ending in a mutant stem-loop that does not bind SLBP. Capped luciferase mRNAs ending in the stem-loop were injected into Xenopus oocytes after overexpression of either xSLBP1 or xSLBP2. Overexpression of xSLBP1 in the oocytes stimulated translation, while overexpression of xSLBP2 reduced translation of the luciferase mRNA ending in the histone stem-loop. A small region in the N-terminal portion of xSLBP1 is required to stimulate translation both in vivo and in vitro. An MS2-human SLBP1 fusion protein can activate translation of a reporter mRNA ending in an MS2 binding site, indicating that xSLBP1 only needs to be recruited to the 3' end of the mRNA but does not need to be directly bound to the histone stem-loop to activate translation.

Indexed as

mRNA Cleavage and Polyadenylation FactorsNuclear ProteinsProtein BiosynthesisRNA, MessengerXenopus ProteinsAnimalsBinding SitesFemaleHistonesHumansRecombinant Fusion ProteinsRNA-Binding ProteinsXenopusHistonesmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsRecombinant Fusion ProteinsRNA-Binding ProteinsRNA, MessengerSLBP1 protein, XenopusSLBP protein, humanXenopus Proteins

Identifiers

PMID12242288
PMCPMC139811
OpenAlexW2151872074

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.