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Expression profile of hsp31∆, hsp32∆, hsp33∆ during diauxic shift

ABSTRACT: The yeast Hsp31 mini-family proteins (Hsp31, Hsp32, Hsp33, Hsp34) belong to the highly conserved DJ-1 superfamily. The human DJ-1 protein is associated with cancer and neurodegenerative disorders, such as Parkinson’s disease. However, the precise function of human and yeast DJ-1 proteins is unclear. Here we show that the yeast DJ-1 homologs have a role in diauxic-shift, characterized by metabolic reprogramming due to glucose limitation. We find that the Hsp31 genes are strongly induced in diauxic-shift and in stationary phase (SP), and that deletion of these genes reduces chronological lifespan, impairs transcriptional reprogramming at diauxic-shift, and impairs the acquisition of several typical characteristics of SP, including autophagy induction. In addition, under carbon starvation, the HSP31 family gene deletion strains display impaired autophagy, disrupted TORC1 localization to P-bodies, and caused abnormal TORC1-mediated Atg13 phosphorylation. Repression of TORC1 by rapamycin in the gene deletion strains completely reversed their sensitivity to heat shock. Altogether, our data indicate that Hsp31 mini-family is required for diauxic-shift reprogramming and cell survival in SP, and plays a role upstream of TORC1. The enhanced understanding of the cellular function of these genes sheds light into the biological role of other members of the superfamily, including DJ-1, which is an attractive target for therapeutic intervention in cancer and in Parkinson’s disease. hsp31∆, hsp32∆, hsp33∆ are compared with its parental strain BY4741. We used One-Color Microarray-Based Gene Expression Analysis Low Input Quick Amp Labeling from Agilent.

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE56124 | GEO | 2014/03/25

SECONDARY ACCESSION(S): PRJNA242536

REPOSITORIES: GEO

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Project description:Yeast (Saccharomyces cerevisea) has served as a key model system in biology and as a benchmark for “omics” technology. Although near-complete proteomes of log phase yeast have been measured, protein abundance in yeast is dynamic, particularly during the transition from log to stationary phase. Defining the dynamics of proteomic changes during this transition, termed the diauxic shift, is important to understand the basic biology of proliferative versus quiescent cells. Here, we perform temporal quantitative proteomics to fully capture protein induction and repression during the diauxic shift. Accurate and sensitive quantitation at a high temporal resolution and depth of proteome coverage was achieved using TMT10 reagents and LC-MS3 analysis on an Orbitrap Fusion tribrid mass spectrometer deploying synchronous precursor selection (SPS). We devised a simple template matching strategy to reveal temporal patterns of protein induction and repression. Within these groups are functionally distinct groups of proteins such as those of glyoxylate metabolism, as well as many proteins of unknown function not previously associated with the diauxic shift (e.g. YNR034W-A and FMP16). We also perform a dual time-course to determine Hap2-dependent proteins during the diauxic shift. These data serve as an important basic model for fermentative versus respiratory growth of yeast and other eukaryotes and are a benchmark for temporal quantitative proteomics.st (Saccharomyces cerevisea) has served as a key model system in biology and as a benchmark for “omics” technology. Although near-complete proteomes of log phase yeast have been measured, protein abundance in yeast is dynamic, particularly during the transition from log to stationary phase. Defining the dynamics of proteomic changes during this transition, termed the diauxic shift, is important to understand the basic biology of proliferative versus quiescent cells. Here, we perform temporal quantitative proteomics to fully capture protein induction and repression during the diauxic shift. Accurate and sensitive quantitation at a high temporal resolution and depth of proteome coverage was achieved using TMT10 reagents and LC-MS3 analysis on an Orbitrap Fusion tribrid mass spectrometer deploying synchronous precursor selection (SPS). We devised a simple template matching strategy to reveal temporal patterns of protein induction and repression. Within these groups are functionally distinct groups of proteins such as those of glyoxylate metabolism, as well as many proteins of unknown function not previously associated with the diauxic shift (e.g. YNR034W-A and FMP16). We also perform a dual time-course to determine Hap2-dependent proteins during the diauxic shift. These data serve as an important basic model for fermentative versus respiratory growth of yeast and other eukaryotes and are a benchmark for temporal quantitative proteomics.

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Expression profile of hsp31∆, hsp32∆, hsp33∆ during diauxic shift

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