Evidence map›Paper›PMID 35857444›Full record

ArticleScience advances2022

HP1 oligomerization compensates for low-affinity H3K9me recognition and provides a tunable mechanism for heterochromatin-specific localization.

Saikat Biswas, Ziyuan Chen, Joshua D Karslake, Ali Farhat, Amanda Ames, Gulzhan Raiymbek, Lydia Freddolino, Julie S Biteen, Kaushik Ragunathan

Abstract read
In one paragraph

Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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  16. Genome control by SMC complexes.Nature reviews. Molecular cell biology · 2023
    Review
  17. 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

9 authors.

Saikat BiswasDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.ORCID 0000-0001-9762-2962
Ziyuan ChenDepartment of Biophysics, University of Michigan, Ann Arbor, MI 48104, USA.ORCID 0000-0003-2832-945X
Joshua D KarslakeDepartment of Biophysics, University of Michigan, Ann Arbor, MI 48104, USA.ORCID 0000-0002-3818-2888
Ali FarhatDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, MI 48109, USA.ORCID 0000-0003-0488-044X
Amanda AmesDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.ORCID 0000-0001-7105-6210
Gulzhan RaiymbekDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.ORCID 0000-0003-4983-0091
Lydia FreddolinoDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.ORCID 0000-0002-5821-4226
Julie S BiteenDepartment of Biophysics, University of Michigan, Ann Arbor, MI 48104, USA.ORCID 0000-0003-2038-6484
Kaushik RagunathanDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.ORCID 0000-0001-9762-2962

Funding

PREDOCTORAL TRAINING IN GENETICST32GM007544 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MORAN, JOHN V. · 1985 to 2022
$11.3M
Heterochromatin dynamics during inheritance and adaptationR35GM137832 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Kaushik Ragunathan · 2020 to 2026
$3.2M
High-Performance Computing Cluster for Biomedical ResearchS10OD026825 · OD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ATHEY, BRIAN DAVID · 2020 to 2020
$600k
NIGMS NIH HHS R35 GM137832NIGMS NIH HHS T32 GM007544NIH HHS S10 OD026825
6 · The paper itself

Abstract

HP1 proteins traverse a complex and crowded chromatin landscape to bind with low affinity but high specificity to histone H3K9 methylation (H3K9me) and form transcriptionally inactive genomic compartments called heterochromatin. Here, we visualize single-molecule dynamics of an HP1 homolog, the fission yeast Swi6, in its native chromatin environment. By tracking single Swi6 molecules, we identify mobility states that map to discrete biochemical intermediates. Using Swi6 mutants that perturb H3K9me recognition, oligomerization, or nucleic acid binding, we determine how each biochemical property affects protein dynamics. We estimate that Swi6 recognizes H3K9me3 with ~94-fold specificity relative to unmodified nucleosomes in living cells. While nucleic acid binding competes with Swi6 oligomerization, as few as four tandem chromodomains can overcome these inhibitory effects to facilitate Swi6 localization at heterochromatin formation sites. Our studies indicate that HP1 oligomerization is essential to form dynamic, higher-order complexes that outcompete nucleic acid binding to enable specific H3K9me recognition.

Identifiers

PMID35857444
PMCPMC9269880

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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.