Evidence map›Paper›PMID 16055700›Full record

ArticleMolecular and cellular biology2005

Subunit contributions to histone methyltransferase activities of fly and worm polycomb group complexes.

Carrie S Ketel, Erica F Andersen, Marcus L Vargas, Jinkyo Suh, Susan Strome, Jeffrey A Simon

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
2.8field-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

99 citing papers in PubMed, 214 citations in OpenAlex.

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  7. iScience · 2022
    Article
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. The Role of Polycomb Group Protein BMI1 in DNA Repair and Genomic Stability.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review

39 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

6 authors at 1 institution in 1 country.

Carrie S KetelDepartment of Genetics, Cell Biology and Development, University of Minnesota, Minneapolis, 55455, USA.
Erica F Andersen
Marcus L Vargas
Jinkyo Suh
Susan Strome
Jeffrey A Simon
University of Minnesota · US

Funding

IMMUNOLOGIC STUDY OF GERM GRANULES IN C. ELEGANS EMBRY0SR01GM034059 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI STROME, SUSAN · 1985 to 2020
$8.9M
TRANSCRIPTIONAL REPRESSION BY POLYCOMB GROUP PRODUCTSR01GM049850 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI SIMON, JEFFREY A · 1996 to 2017
$4.8M
DEVELOPMENTAL BIOLOGY TRAINING PROGRAMT32HD007480 · NICHD · UNIVERSITY OF MINNESOTA TWIN CITIES · PI O'CONNOR, MICHAEL BRENDAN · 1995 to 2011
$1.2M
NICHD NIH HHS HD07480NICHD NIH HHS T32 HD007480NIGMS NIH HHS GM34059NIGMS NIH HHS GM49850NIGMS NIH HHS R01 GM034059NIGMS NIH HHS R01 GM049850
6 · The paper itself

Abstract

The ESC-E(Z) complex of Drosophila melanogaster Polycomb group (PcG) repressors is a histone H3 methyltransferase (HMTase). This complex silences fly Hox genes, and related HMTases control germ line development in worms, flowering in plants, and X inactivation in mammals. The fly complex contains a catalytic SET domain subunit, E(Z), plus three noncatalytic subunits, SU(Z)12, ESC, and NURF-55. The four-subunit complex is >1,000-fold more active than E(Z) alone. Here we show that ESC and SU(Z)12 play key roles in potentiating E(Z) HMTase activity. We also show that loss of ESC disrupts global methylation of histone H3-lysine 27 in fly embryos. Subunit mutations identify domains required for catalytic activity and/or binding to specific partners. We describe missense mutations in surface loops of ESC, in the CXC domain of E(Z), and in the conserved VEFS domain of SU(Z)12, which each disrupt HMTase activity but preserve complex assembly. Thus, the E(Z) SET domain requires multiple partner inputs to produce active HMTase. We also find that a recombinant worm complex containing the E(Z) homolog, MES-2, has robust HMTase activity, which depends upon both MES-6, an ESC homolog, and MES-3, a pioneer protein. Thus, although the fly and mammalian PcG complexes absolutely require SU(Z)12, the worm complex generates HMTase activity from a distinct partner set.

Indexed as

AnimalsBaculoviridaeBlotting, WesternCaenorhabditis elegansCatalytic DomainChromatinChromosomal Proteins, Non-HistoneDNA MethylationDNA Mutational AnalysisDose-Response Relationship, DrugDrosophila melanogasterDrosophila ProteinsHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesHumansCaf1-55 protein, DrosophilaChromatinChromosomal Proteins, Non-HistoneDrosophila Proteinsesc protein, DrosophilaHistone-Lysine N-MethyltransferaseHistone MethyltransferasesHistonesLysineMacromolecular SubstancesMolecular ChaperonesMultiprotein ComplexesPc protein, DrosophilaPolycomb Repressive Complex 1Polycomb Repressive Complex 2Protein MethyltransferasesRecombinant Fusion ProteinsRecombinant ProteinsRepressor ProteinsRetinoblastoma-Binding Protein 4Su(z)12 protein, Drosophila

Identifiers

PMID16055700
PMCPMC1190254
OpenAlexW2149098354

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.