Evidence map›Paper›PMID 20635087›Full record

ArticleCurrent genetics2010

Mutational analysis of the C-terminal FATC domain of Saccharomyces cerevisiae Tra1.

Stephen M T Hoke, A Irina Mutiu, Julie Genereaux, Stephanie Kvas, Michael Buck, Michael Yu, Gregory B Gloor, Christopher J Brandl

Open access · hybridAbstract read
In one paragraph

Article in Current genetics, 2010. 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
1.2field-weighted citation impact, top 22% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  6. The Pseudokinase Domain ofG3 (Bethesda, Md.) · 2018
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  10. Review
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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

8 authors at 3 institutions in 2 countries.

Stephen M T HokeDepartment of Biochemistry, University of Western Ontario, London, Canada.
A Irina Mutiu
Julie Genereaux
Stephanie Kvas
Michael Buck
Michael Yu
Gregory B Gloor
Christopher J Brandl
Western University · CAState University of New York · USUniversity at Buffalo, State University of New York · US

Funding

Canadian Institutes of Health Research MOP10845
6 · The paper itself

Abstract

Tra1 is a component of the Saccharomyces cerevisiae SAGA and NuA4 complexes and a member of the PIKK family, which contain a C-terminal phosphatidylinositol 3-kinase-like (PI3K) domain followed by a 35-residue FATC domain. Single residue changes of L3733A and F3744A, within the FATC domain, resulted in transcriptional changes and phenotypes that were similar but not identical to those caused by mutations in the PI3K domain or deletions of other SAGA or NuA4 components. The distinct nature of the FATC mutations was also apparent from the additive effect of tra1-L3733A with SAGA, NuA4, and tra1 PI3K domain mutations. Tra1-L3733A associates with SAGA and NuA4 components and with the Gal4 activation domain, to the same extent as wild-type Tra1; however, steady-state levels of Tra1-L3733A were reduced. We suggest that decreased stability of Tra1-L3733A accounts for the phenotypes since intragenic suppressors of tra1-L3733A restored Tra1 levels, and reducing wild-type Tra1 led to comparable growth defects. Also supporting a key role for the FATC domain in the structure/function of Tra1, addition of a C-terminal glycine residue resulted in decreased association with Spt7 and Esa1, and loss of cellular viability. These findings demonstrate the regulatory potential of mechanisms targeting the FATC domains of PIKK proteins.

Indexed as

Gene Expression Regulation, FungalProtein Interaction Domains and MotifsAlcohol OxidoreductasesAmino Acid SequenceBase SequenceBlotting, WesternDNA-Binding ProteinsDNA, FungalDNA Mutational AnalysisGene ExpressionGene Expression ProfilingHistone AcetyltransferasesMutationPhosphatidylinositol 3-KinasePoint MutationPolymerase Chain ReactionAlcohol OxidoreductasesC-terminal binding proteinDNA-Binding ProteinsDNA, FungalHistone AcetyltransferasesNuA4 protein, S cerevisiaePhosphatidylinositol 3-KinaseSaccharomyces cerevisiae ProteinsSAGA complex, S cerevisiaeTRA1 protein, S cerevisiaeTrans-Activators

Identifiers

PMID20635087
PMCPMC2943577
OpenAlexW2075943942

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.