Evidence map›Paper›PMID 16287868›Full record

ArticleMolecular and cellular biology2005

Histone H3 Ser10 phosphorylation-independent function of Snf1 and Reg1 proteins rescues a gcn5- mutant in HIS3 expression.

Yang Liu, Xinjing Xu, Soumya Singh-Rodriguez, Yan Zhao, Min-Hao Kuo

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  16. SNF1/AMPK pathways in yeast.Frontiers in bioscience : a journal and virtual library · 2008
    Review
  17. Review
  18. 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

5 authors at 2 institutions in 2 countries.

Yang Liu401 BCH Building, Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824. kuom@msu.edu.
Xinjing Xu
Soumya Singh-Rodriguez
Yan Zhao
Min-Hao Kuo
Michigan State University · USInstitut thématique Génétique, génomique et bioinformatique · FR

Funding

HISTONE ACETYLTRANSFERASE AND TRANSCRIPTIONAL REGULATIONR01GM062282 · NIGMS · MICHIGAN STATE UNIVERSITY · PI KUO, MIN-HAO · 2001 to 2005
$1.2M
NIGMS NIH HHS R01 GM062282NIGMS NIH HHS R01 GM62282
6 · The paper itself

Abstract

Gcn5 protein is a prototypical histone acetyltransferase that controls transcription of multiple yeast genes. To identify molecular functions that act downstream of or in parallel with Gcn5 protein, we screened for suppressors that rescue the transcriptional defects of HIS3 caused by a catalytically inactive mutant Gcn5, the E173H mutant. One bypass of Gcn5 requirement gene (BGR) suppressor was mapped to the REG1 locus that encodes a semidominant mutant truncated after amino acid 740. Reg1(1-740) protein does not rescue the complete knockout of GCN5, nor does it suppress other gcn5- defects, including the inability to utilize nonglucose carbon sources. Reg1(1-740) enhances HIS3 transcription while HIS3 promoter remains hypoacetylated, indicating that a noncatalytic function of Gcn5 is targeted by this suppressor protein. Reg1 protein is a major regulator of Snf1 kinase that phosphorylates Ser10 of histone H3. However, whereas Snf1 protein is important for HIS3 expression, replacing Ser10 of H3 with alanine or glutamate neither attenuates nor augments the BGR phenotypes. Overproduction of Snf1 protein also preferentially rescues the E173H allele. Biochemically, both Snf1 and Reg1(1-740) proteins copurify with Gcn5 protein. Snf1 can phosphorylate recombinant Gcn5 in vitro. Together, these data suggest that Reg1 and Snf1 proteins function in an H3 phosphorylation-independent pathway that also involves a noncatalytic role played by Gcn5 protein.

Indexed as

AllelesAmino Acid SequenceBase SequenceGene Expression Regulation, FungalGlutamic AcidHistone AcetyltransferasesHistonesHydro-LyasesMolecular Sequence DataMutationp300-CBP-Associated FactorPhenotypePhosphoprotein PhosphatasesPhosphoserineProtein BindingProtein Phosphatase 1GCN5 protein, S cerevisiaeGlutamic AcidHistone AcetyltransferasesHistonesHydro-Lyasesimidazoleglycerolphosphate dehydratasep300-CBP-Associated FactorPhosphoprotein PhosphatasesPhosphoserineProtein Phosphatase 1Protein Serine-Threonine KinasesREG1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSNF1-related protein kinases

Identifiers

PMID16287868
PMCPMC1291248
OpenAlexW2069824029

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.