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Effects of abolishing Whi2 on the proteome and nitrogen catabolite repression-sensitive protein production - Proteomics of P1 and P1-whi2 strains in SCCSH and SCME liquid media.

ABSTRACT: The associated files are mass spec data of proteins from liquid cultures of Saccharomyces cerevisiae P1 and P1-whi2 strains.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Karel Harant

LAB HEAD: Zdena Palková

PROVIDER: PXD028004 | Pride | 2021-11-29

REPOSITORIES: Pride

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Project description:In yeast physiology, a commonly used reference condition for many experiments, including those involving nitrogen catabolite repression (NCR), is growth in synthetic complete (SC) medium. Four SC formulations, SCCSH,1990, SCCSH,1994, SCCSH,2005, and SCME, have been used interchangeably as the nitrogen-rich medium of choice [Cold Spring Harbor Yeast Course Manuals (SCCSH) and a formulation in the methods in enzymology (SCME)]. It has been tacitly presumed that all of these formulations support equivalent responses. However, a recent report concluded that (i) TorC1 activity is downregulated by the lower concentration of primarily leucine in SCME relative to SCCSH. (ii) The Whi2-Psr1/2 complex is responsible for this downregulation. TorC1 is a primary nitrogen-responsive regulator in yeast. Among its downstream targets is control of NCR-sensitive transcription activators Gln3 and Gat1. They in turn control production of catabolic transporters and enzymes needed to scavenge poor nitrogen sources (e.g., Proline) and activate autophagy (ATG14). One of the reporters used in Chen et al. was an NCR-sensitive DAL80-GFP promoter fusion. This intrigued us because we expected minimal if any DAL80 expression in SC medium. Therefore, we investigated the source of the Dal80-GFP production and the proteomes of wild-type and whi2Δ cells cultured in SCCSH and SCME. We found a massive and equivalent reorientation of amino acid biosynthetic proteins in both wild-type and whi2Δ cells even though both media contained high overall concentrations of amino acids. Gcn2 appears to play a significant regulatory role in this reorientation. NCR-sensitive DAL80 expression and overall NCR-sensitive protein production were only marginally affected by the whi2Δ. In contrast, the levels of 58 proteins changed by an absolute value of log2 between 3 and 8 when Whi2 was abolished relative to wild type. Surprisingly, with only two exceptions could those proteins be related in GO analyses, i.e., GO terms associated with carbohydrate metabolism and oxidative stress after shifting a whi2Δ from SCCSH to SCME for 6 h. What was conspicuously missing were proteins related by TorC1- and NCR-associated GO terms.

			Action	DRS
	559-1.CID.ITMS.peak.apl	Other
	559-1.HCD.ITMS.peak.apl	Other
	559-1.raw	Raw
	559-10.CID.ITMS.peak.apl	Other
	559-10.HCD.ITMS.peak.apl	Other

Dataset Information

Effects of abolishing Whi2 on the proteome and nitrogen catabolite repression-sensitive protein production - Proteomics of P1 and P1-whi2 strains in SCCSH and SCME liquid media.

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