Evidence map›Paper›PMID 12588979›Full record

ArticleMolecular and cellular biology2003

Phosphorylation of stem-loop binding protein (SLBP) on two threonines triggers degradation of SLBP, the sole cell cycle-regulated factor required for regulation of histone mRNA processing, at the end of S phase.

Lianxing Zheng, Zbigniew Dominski, Xiao-Cui Yang, Phillip Elms, Christy S Raska, Christoph H Borchers, William F Marzluff

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
2.4field-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

66 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Polyadenylation of canonical histone H3.1 in carcinogenesis.Advances in pharmacology (San Diego, Calif.) · 2023
    Article
  8. Article
  9. Nucleosome proteostasis and histone turnover.Frontiers in molecular biosciences · 2022
    Review
  10. 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
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. RNA Decay Factor UPF1 Promotes Protein Decay: A Hidden Talent.BioEssays : news and reviews in molecular, cellular and developmental biology · 2018
    Review
  18. Article
  19. Article
  20. "FEM1"nism controls SLBP stability during cell cycle.Cell cycle (Georgetown, Tex.) · 2017
    Article

6 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

7 authors at 1 institution in 1 country.

Lianxing ZhengDepartment of Biochemistry and Biophysics. Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, North Carolina 27599, USA.
Zbigniew Dominski
Xiao-Cui Yang
Phillip Elms
Christy S Raska
Christoph H Borchers
William 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 GM 29832NIGMS NIH HHS R01 GM029832
6 · The paper itself

Abstract

The replication-dependent histone mRNAs, the only eukaryotic mRNAs that do not have poly(A) tails, are present only in S-phase cells. Coordinate posttranscriptional regulation of histone mRNAs is mediated by the stem-loop at the 3' end of histone mRNAs. The protein that binds the 3' end of histone mRNA, stem-loop binding protein (SLBP), is required for histone pre-mRNA processing and is involved in multiple aspects of histone mRNA metabolism. SLBP is also regulated during the cell cycle, accumulating as cells enter S phase and being rapidly degraded as cells exit S phase. Mutation of any residues in a TTP sequence (amino acids 60 to 62) or mutation of a consensus cyclin binding site (amino acids 99 to 104) stabilizes SLBP in G2 and mitosis. These two threonines are phosphorylated in late S phase, as determined by mass spectrometry (MS) of purified SLBP from late S-phase cells, triggering SLBP degradation. Cells that express a stable SLBP still degrade histone mRNA at the end of S phase, demonstrating that degradation of SLBP is not required for histone mRNA degradation. Nuclear extracts from G1 and G2 cells are deficient in histone pre-mRNA processing, which is restored by addition of recombinant SLBP, indicating that SLBP is the only cell cycle-regulated factor required for histone pre-mRNA processing.

Indexed as

mRNA Cleavage and Polyadenylation FactorsNuclear ProteinsXenopus ProteinsAmino Acid MotifsAmino Acid SequenceAnimalsBlotting, WesternCell CycleCell NucleusChromatography, GasChromatography, LiquidCloning, MolecularDNA, ComplementaryG1 PhaseG2 PhaseHeLa CellsDNA, ComplementaryHistonesmRNA Cleavage and Polyadenylation FactorsNuclear ProteinsProlineRecombinant ProteinsRNA-Binding ProteinsRNA, MessengerSLBP1 protein, XenopusSLBP protein, humanThreonineXenopus Proteins

Identifiers

PMID12588979
PMCPMC151715
OpenAlexW1966536060

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.