Yeast Tdh3 (Glyceraldehyde 3-Phosphate Dehydrogenase) Is a Sir2-Interacting Factor That Regulates Transcriptional Silencing and rDNA Recombination

Ringel, Alison E.; Ryznar, Rebecca; Picariello, Hannah; Huang, Kuan‐lin; Lazarus, Asmitha; Holmes, Scott G.

doi:10.1371/journal.pgen.1003871

Cited by 62 publications

(86 citation statements)

References 74 publications

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“…glyceraldehyde 3-phosphate dehydrogenase/Tdh3, pyruvate kinase/Cdc19, homocitrate synthase/Lys20,Lys21) and protein chaperones (e.g. the HSP70 chaperones Ssa1 and Ssa2), there is evidence that they have active roles in transcription and DNA repair [46][47][48][49][50] . Furthermore, the binding scores of some metabolic enzymes changed upon treatment with HU (Supplementary Table 2), indicating that their interaction with chromatin is not constitutive.…”

Section: Discussionmentioning

confidence: 99%

Decoding the chromatin proteome of a single genomic locus by DNA sequencing

Korthout

Poramba‐Liyanage

Verzijlbergen

et al. 2017

Preprint

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Transcription, replication and repair involve interactions of specific genomic loci with many different proteins. How these interactions are orchestrated at any given location and under changing cellular conditions is largely unknown because systematically measuring protein-DNA interactions at a specific locus in the genome is challenging. To address this problem, we developed Epi-Decoder, a Tag-ChIPBarcode-Seq technology in budding yeast to identify and quantify in an unbiased and systematic manner the proteome of an individual genomic locus. Epi-Decoder is orthogonal to proteomics approaches because it does not rely on mass spectrometry but instead takes advantage of DNA sequencing. Analysis of the proteome of a transcribed locus proximal to an origin of replication revealed more than 400 proteins. Moreover, replication stress induced changes in local chromatin-proteome composition prior to local origin firing, affecting replication proteins as well as transcription proteins. Epi-Decoder will enable the delineation of complex and dynamic protein-DNA interactions across many regions of the genome.

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Section: Discussionmentioning

confidence: 99%

Decoding the chromatin proteome of a single genomic locus by DNA sequencing

Korthout

Poramba‐Liyanage

Verzijlbergen

et al. 2017

Preprint

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“…Regulators of GAPDH export such as Sirt1 might also be subjected to redox-modification, which increases the complexity of GAPDH-mediated apoptosis. Similar to the animal system with the Sirt1 binding to GAPDH, in yeast the Sirt1 homologue Sir2 interacts with TDH3 resulting in histone deacetylation and chromatin restructuring (Ringel et al, 2013).…”

Section: Nuclear Functions Of Gapdhmentioning

confidence: 99%

Cytosolic thiol switches regulating basic cellular functions: GAPDH as an information hub?

Hildebrandt¹,

Knuesting²,

Berndt³

et al. 2015

Biological Chemistry

148

131

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Cytosolic glyceraldehyde 3-phosphate dehydrogenase (GAPDH, E.C. 1.2.1.12) is present in all organisms and catalyzes the oxidation of triose phosphate during glycolysis. GAPDH is one of the most prominent cellular targets of oxidative modifications when reactive oxygen and nitrogen species are formed during metabolism and under stress conditions. GAPDH harbors a strictly conserved catalytic cysteine, which is susceptible to a variety of thiol modifications, including S-sulfenylation, S-glutathionylation, S-nitrosylation, and S-sulfhydration. Upon reversible oxidative thiol modification of GAPDH, glycolysis is inhibited leading to a diversion of metabolic flux through the pentose-phosphate cycle to increase NADPH production. Furthermore, oxidized GAPDH may adopt new functions in different cellular compartments including the nucleus, as well as in new microcompartments associated with the cytoskeleton, mitochondria and plasma membrane. This review focuses on the recently discovered mechanism underlying the eminent reactivity between GAPDH and hydrogen peroxide and the subsequent redox-dependent moonlighting functions discriminating between the induction either of adaptive responses and adjustment of metabolism or of cell death in yeast, plants, and mammals. In light of the summarized results, cytosolic GAPDH might function as a sensor for redox signals and an information hub to transduce these signals for appropriate responses.

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“…Examples of the different types of mutations are found for yeast hexokinase (107), galactokinase (108), and some other yeast proteins (18), as well as for mammalian aldolase (109). It has been reported recently that a glyceraldehyde-3-phosphodehydrogenase may play a moonlighting role in S. cerevisiae (110). The isoenzyme Tdh3 has been shown to interact with the sirtuin Sir2 and to facilitate transcriptional silencing at the telomeres.…”

Section: Mutational Analysis and Structural Studiesmentioning

confidence: 99%

The Expanding Landscape of Moonlighting Proteins in Yeasts

Gancedo

Flores

Gancedo

2016

Microbiol Mol Biol Rev

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SUMMARYMoonlighting proteins are multifunctional proteins that participate in unrelated biological processes and that are not the result of gene fusion. A certain number of these proteins have been characterized in yeasts, and the easy genetic manipulation of these microorganisms has been useful for a thorough analysis of some cases of moonlighting. As the awareness of the moonlighting phenomenon has increased, a growing number of these proteins are being uncovered. In this review, we present a crop of newly identified moonlighting proteins from yeasts and discuss the experimental evidence that qualifies them to be classified as such. The variety of moonlighting functions encompassed by the proteins considered extends from control of transcription to DNA repair or binding to plasminogen. We also discuss several questions pertaining to the moonlighting condition in general. The cases presented show that yeasts are important organisms to be used as tools to understand different aspects of moonlighting proteins.

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Yeast Tdh3 (Glyceraldehyde 3-Phosphate Dehydrogenase) Is a Sir2-Interacting Factor That Regulates Transcriptional Silencing and rDNA Recombination

Cited by 62 publications

References 74 publications

Decoding the chromatin proteome of a single genomic locus by DNA sequencing

Decoding the chromatin proteome of a single genomic locus by DNA sequencing

Cytosolic thiol switches regulating basic cellular functions: GAPDH as an information hub?

The Expanding Landscape of Moonlighting Proteins in Yeasts

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