Evidence map›Paper›PMID 17447102›Full record

ArticleMolecular genetics and genomics : MGG2007

The role of histone ubiquitylation and deubiquitylation in gene expression as determined by the analysis of an HTB1(K123R) Saccharomyces cerevisiae strain.

A Irina Mutiu, Stephen M T Hoke, Julie Genereaux, Gaoyang Liang, Christopher J Brandl

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In one paragraph

Article in Molecular genetics and genomics : MGG, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Histone modifications as regulators of life and death inMicrobial cell (Graz, Austria) · 2015
    Review
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  15. Review
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  17. Ubiquitination of histone H2B regulates chromatin dynamics by enhancing nucleosome stability.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
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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

5 authors at 2 institutions in 2 countries.

A Irina MutiuDepartment of Biochemistry, Schulich School of Medicine and Dentistry, University of Western Ontario, London, Canada.
Stephen M T Hoke
Julie Genereaux
Gaoyang Liang
Christopher J Brandl
Western University · CAUniversity of North Carolina at Chapel Hill · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Saccharomyces cerevisiae histone H2B is ubiquitylated at lysine 123 in a process requiring the E2-ubiquitin conjugase, Rad6. We have analyzed gene expression in a strain containing a variant of histone H2B with lysine 123 converted to arginine to address the mechanisms by which ubiquitylation and deubiquitylation of histone H2B affect gene expression. The SAGA complex component, Ubp8, is one of two proteases that remove the ubiquitin moiety at lysine 123. We show that changes in gene expression observed upon deletion of ubp8 are suppressed by htb1 ( K123R ), which provides genetic evidence that Ubp8 alters gene expression through deubiquitylation of histone H2B. Microarray analyses of the htb1 ( K123R ) strain show that loss of histone ubiquitylation results in a twofold or greater change in expression of approximately 1.5% of the protein coding genes with approximately 75% of these increasing. For genes in which ubiquitylation represses expression, ubiquitylation principally acts through its effects on histone methylation. In contrast, decreased expression of the CWP1 gene was not paralleled by deletions of methyltransferase components and is thus likely independent of methylation. Finally, by comparing gene expression changes in the htb1 ( K123R ) strain with those in a strain deleted for rad6, we conclude that lysine 123 affects transcription primarily because of it being a site of ubiquitylation.

Indexed as

Gene Expression Regulation, FungalAmino Acid SubstitutionAmino Acid Transport SystemsArginineEndopeptidasesHistone-Lysine N-MethyltransferaseHistonesLysineMembrane GlycoproteinsMethylationMutationNuclear ProteinsOligonucleotide Array Sequence AnalysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsADA2 protein, S cerevisiaeAmino Acid Transport SystemsArginineCWP1 protein, S cerevisiaeDot1 protein, S cerevisiaeEndopeptidasesGAP1 protein, S cerevisiaeHistone-Lysine N-MethyltransferaseHistonesLysineMembrane GlycoproteinsNuclear ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsUbiquitinUBP8 protein, S cerevisiae

Identifiers

PMID17447102
OpenAlexW2021983747

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.