Evidence map›Paper›PMID 38963485›Full record

ReviewSub-cellular biochemistry2024

The Core Complex of Yeast COMPASS and Human Mixed-Lineage Leukemia (MLL), Structure, Function, and Recognition of the Nucleosome.

Uhn-Soo Cho

Abstract readReview
PubMed Publisher
In one paragraph

Review in Sub-cellular biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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

1 author.

Uhn-Soo ChoDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI, USA. uhnsoo@med.umich.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yeast COMPASS (complex of proteins associated with Set1) and human MLL (mixed-lineage leukemia) complexes are histone H3 lysine 4 methyltransferases with critical roles in gene regulation and embryonic development. Both complexes share a conserved C-terminal SET domain, responsible for catalyzing histone H3 K4 methylation on nucleosomes. Notably, their catalytic activity toward nucleosomes is enhanced and optimized with assembly of auxiliary subunits. In this review, we aim to illustrate the recent X-ray and cryo-EM structures of yeast COMPASS and human MLL1 core complexes bound to either unmodified nucleosome core particle (NCP) or H2B mono-ubiquitinated NCP (H2Bub.NCP). We further delineate how each auxiliary component of the complex contributes to the NCP and ubiquitin recognition to maximize the methyltransferase activity.

Indexed as

Histone-Lysine N-MethyltransferaseMyeloid-Lymphoid Leukemia ProteinNucleosomesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCryoelectron MicroscopyHistonesHumansHistone-Lysine N-MethyltransferaseHistonesKMT2A protein, humanMyeloid-Lymphoid Leukemia ProteinNucleosomesSaccharomyces cerevisiae ProteinsSET1 protein, S cerevisiaeCOMPASSH2B K120 (K123 in yeast) mono-ubiquitinated nucleosome (H2Bub.NCP)H3 Lys4 methyltransferaseMLLNucleosomal core particle (NCP)SET domainSingle-particle electron cryomicroscopy (cryo-EM)X-ray crystallography

Identifiers

PMID38963485

What OpenQuestion holds

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Registered trials

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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.