The Saccharomyces cerevisiae linker histone Hho1p is essential for chromatin compaction in stationary phase and is displaced by transcription.

Proc Natl Acad Sci U S A

Department of Microbial, Biochemical, and Food Biotechnology, University of the Free State, P.O. Box 339, Bloemfontein 9300, South Africa.

Published: September 2008

The importance of core histones in the regulation of DNA function by chromatin is clear. However, little is known about the role of the linker histone. We investigated the role of H1 in Saccharomyces cerevisiae during extensive transcriptional reprogramming in stationary phase. Although the levels of linker histone Hho1p remained constant during growth to semiquiescence, there was a genome-wide increase in binding to chromatin. Hho1p was essential for compaction of chromatin in stationary phase, but not for general transcriptional repression. A clear, genome-wide anticorrelation was seen between the level of bound Hho1p and gene expression. Surprisingly, the rank order of gene activity was maintained even in the absence of Hho1p. Based on these findings, we suggest that linker histone Hho1p has a limited role in transcriptional regulation and that the dynamically exchanging linker histone may be evicted from chromatin by transcriptional activity.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2567454PMC
http://dx.doi.org/10.1073/pnas.0806337105DOI Listing

Publication Analysis

Top Keywords

linker histone
20
histone hho1p
12
stationary phase
12
saccharomyces cerevisiae
8
hho1p essential
8
hho1p
6
linker
5
histone
5
chromatin
5
cerevisiae linker
4

Similar Publications

Structural insights into how Cas9 targets nucleosomes.

Nat Commun

December 2024

Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Tokyo, Japan.

The CRISPR-associated endonuclease Cas9 derived from prokaryotes is used as a genome editing, which targets specific genomic loci by single guide RNAs (sgRNAs). The eukaryotes, the target of genome editing, store their genome DNA in chromatin, in which the nucleosome is a basic unit. Despite previous structural analyses focusing on Cas9 cleaving free DNA, structural insights into Cas9 targeting of DNA within nucleosomes are limited, leading to uncertainties in understanding how Cas9 operates in the eukaryotic genome.

View Article and Find Full Text PDF

High carbohydrate availability promotes malic acid accumulation in fleshy fruits, but the underlying mechanism is not known. Here, we show that antisense repression of ALDOSE-6-PHOSPHATE REDUCTASE in apple (Malus domestica) decreases the concentrations of sorbitol and malate and the transcript levels of several genes involved in vacuolar malate transport, including the aluminum-activated malate transporter (ALMT) gene MdALMT9 (Ma1), the P-ATPase gene MdPH5, the MYB transcription factor gene MdMYB73, and the cold-induced basic helix-loop-helix transcription factor gene MdCIbHLH1, in fruit and leaves. We identified a linker histone H1 variant, MdH1.

View Article and Find Full Text PDF

Histone deacetylase inhibitors (HDACi) are established anticancer drugs, especially in hematological cancers. This study aimed to design, synthesize, and evaluate a set of HDACi featuring a pentyloxyamide connecting unit linker region and substituted phenylthiazole cap groups. A structural optimization program yielded HDACi with nanomolar inhibitory activity against histone deacetylase class I/IIb enzymes.

View Article and Find Full Text PDF

Driving Forces in the Formation of Biocondensates of Highly Charged Proteins: A Thermodynamic Analysis of the Binary Complex Formation.

Biomolecules

November 2024

Institut für Chemie und Biochemie, Freie Universität Berlin, Forschungsbau SupraFab, Altensteinstrasse 23a, 14195 Berlin, Germany.

Article Synopsis
  • The study focuses on the interaction between the positively charged linker histone H1 and the negatively charged chaperone prothymosin α (ProTα), highlighting their strong binding in physiological conditions.
  • The analysis employs a thermodynamic model that considers the influence of counterion release and hydration on the complex formation.
  • The findings reveal that the binding energy is primarily driven by the release of counterions from ProTα, while changes in water interactions and conformational constraints contribute to a significant negative change in free energy.
View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!