Evidence map›Paper›PMID 38366024›Full record

ArticleGenetics2024

Histone variant H2A.Z and linker histone H1 influence chromosome condensation in Saccharomyces cerevisiae.

Anna M Rogers, Nola R Neri, Lorencia Chigweshe, Scott G Holmes

Open access · greenAbstract read
In one paragraph

Article in Genetics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 47% 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

2 citing papers in PubMed, 1 citations in OpenAlex.

  1. Article
  2. 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

4 authors at 1 institution in 1 country.

Anna M RogersDepartment of Molecular Biology and Biochemistry, Wesleyan University, Middletown, CT 06459, USA.
Nola R NeriDepartment of Molecular Biology and Biochemistry, Wesleyan University, Middletown, CT 06459, USA.
Lorencia ChigwesheDepartment of Molecular Biology and Biochemistry, Wesleyan University, Middletown, CT 06459, USA.
Scott G HolmesDepartment of Molecular Biology and Biochemistry, Wesleyan University, Middletown, CT 06459, USA.ORCID 0000-0002-0154-198X
Wesleyan University · US

Funding

Functional interaction of histone H1 with the core nucleosomeR15GM102824 · NIGMS · WESLEYAN UNIVERSITY · PI HOLMES, SCOTT G · 2012 to 2012
$374k
NIGMS NIH HHS R15 GM102824NIH HHS 1R15GM102824-01
6 · The paper itself

Abstract

Chromosome condensation is essential for the fidelity of chromosome segregation during mitosis and meiosis. Condensation is associated both with local changes in nucleosome structure and larger-scale alterations in chromosome topology mediated by the condensin complex. We examined the influence of linker histone H1 and variant histone H2A.Z on chromosome condensation in budding yeast cells. Linker histone H1 has been implicated in local and global compaction of chromatin in multiple eukaryotes, but we observe normal condensation of the rDNA locus in yeast strains lacking H1. However, deletion of the yeast HTZ1 gene, coding for variant histone H2A.Z, causes a significant defect in rDNA condensation. Loss of H2A.Z does not change condensin association with the rDNA locus or significantly affect condensin mRNA levels. Prior studies reported that several phenotypes caused by loss of H2A.Z are suppressed by eliminating Swr1, a key component of the SWR complex that deposits H2A.Z in chromatin. We observe that an htz1Δ swr1Δ strain has near-normal rDNA condensation. Unexpectedly, we find that elimination of the linker histone H1 can also suppress the rDNA condensation defect of htz1Δ strains. Our experiments demonstrate that histone H2A.Z promotes chromosome condensation, in part by counteracting activities of histone H1 and the SWR complex.

Indexed as

HistonesSaccharomyces cerevisiae ProteinsChromatinDNA, RibosomalNucleosomesSaccharomyces cerevisiaeChromatinDNA, RibosomalHistonesNucleosomesSaccharomyces cerevisiae Proteinschromatincondensationhistone H1histone H2A.Z

Identifiers

PMID38366024
PMCPMC10990423
OpenAlexW4392390267

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.