Evidence map›Paper›PMID 11238936›Full record

ArticleMolecular and cellular biology2001

Mutations in the RNA binding domain of stem-loop binding protein define separable requirements for RNA binding and for histone pre-mRNA processing.

Z Dominski, J A Erkmann, J A Greenland, W F Marzluff

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

30 citing papers in PubMed, 38 citations in OpenAlex.

  1. Identification and characterization of histones inNAR genomics and bioinformatics · 2021
    Article
  2. Article
  3. Birth and Death of Histone mRNAs.Trends in genetics : TIG · 2017
    Review
  4. Article
  5. Review
  6. 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
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

4 authors at 1 institution in 2 countries.

Z DominskiDepartment of Biochemistry and Biophysics, Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
J A Erkmann
J A Greenland
W F Marzluff
University of North Carolina at Chapel Hill · US

Funding

CONTROL OF HISTONE MRNA SYNTHESISR01GM029832 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI DOMINSKI, ZBIGNIEW, MARZLUFF, WILLIAM F. · 1985 to 2022
$9.0M
NIGMS NIH HHS GM29832NIGMS NIH HHS R01 GM029832
6 · The paper itself

Abstract

Expression of replication-dependent histone genes at the posttranscriptional level is controlled by stem-loop binding protein (SLBP). One function of SLBP is to bind the stem-loop structure in the 3' untranslated region of histone pre-mRNAs and facilitate 3' end processing. Interaction of SLBP with the stem-loop is mediated by the centrally located RNA binding domain (RBD). Here we identify several highly conserved amino acids in the RBD mutation of which results in complete or substantial loss of SLBP binding activity. We also identify residues in the RBD which do not contribute to binding to the stem-loop RNA but instead are required for efficient recruitment of U7 snRNP to histone pre-mRNA. Recruitment of the U7 snRNP to the pre-mRNA also depends on the 20-amino-acid region located immediately downstream of the RBD. A critical region of the RBD contains the sequence YDRY. The tyrosines are required for RNA binding, and the DR dipeptide is essential for processing but not for RNA binding. It is likely that the RBD of SLBP interacts directly with both the stem-loop RNA and other processing factor(s), most likely the U7 snRNP, to facilitate histone pre-mRNA processing.

Indexed as

mRNA Cleavage and Polyadenylation FactorsNuclear ProteinsRNA Processing, Post-TranscriptionalXenopus ProteinsAmino Acid SequenceAnimalsBinding SitesConserved SequenceGenetic Complementation TestHistonesHumansMolecular Sequence DataMutationRibonucleoprotein, U7 Small NuclearRNA-Binding ProteinsRNA, MessengerHistonesmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsRibonucleoprotein, U7 Small NuclearRNA-Binding ProteinsRNA, MessengerRNA PrecursorsSLBP1 protein, XenopusSLBP protein, humanXenopus Proteins

Identifiers

PMID11238936
PMCPMC86798
OpenAlexW2102510549

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.