Proteomics

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SILAC analysis of Δhmt1 yeast - Knockout of the Hmt1p arginine methyltransferase in Saccharomyces cerevisiae leads to the dysregulation of phosphate-associated genes and processes

ABSTRACT: In this study, the proteome-level effects of the deletion of the gene encoding Hmt1p, the predominant yeast arginine methyltransferase, were measured using SILAC (stable isotope labeling by amino acids in cell culture), to clarify if the abundance levels of any proteins were disrupted by systemic loss of arginine methylation. Analysis revealed that numerous proteins were found to be differentially abundant between wild-type yeast and Δhmt1, and functional analysis revealed perturbation of phosphate signalling and repression of the PHO pathway.

OTHER RELATED OMICS DATASETS IN: GSE99869

INSTRUMENT(S): LTQ Orbitrap Velos

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

SUBMITTER: Daniel Yagoub  

LAB HEAD: Marc Roland Wilkins

PROVIDER: PXD004054 | Pride | 2018-11-21

REPOSITORIES: Pride

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A-MQ.txt.zip Txt
B-MQ.txt.zip Txt
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DY_20130611_A10.raw Raw
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Knockout of the Hmt1p Arginine Methyltransferase in <i>Saccharomyces cerevisiae</i> Leads to the Dysregulation of Phosphate-associated Genes and Processes.

Chia Samantha Z SZ   Lai Yu-Wen YW   Yagoub Daniel D   Lev Sophie S   Hamey Joshua J JJ   Pang Chi Nam Ignatius CNI   Desmarini Desmarini D   Chen Zhiliang Z   Djordjevic Julianne T JT   Erce Melissa A MA   Hart-Smith Gene G   Wilkins Marc R MR  

Molecular & cellular proteomics : MCP 20180911 12

Hmt1p is the predominant arginine methyltransferase in <i>Saccharomyces cerevisiae</i> Its substrate proteins are involved in transcription, transcriptional regulation, nucleocytoplasmic transport and RNA splicing. Hmt1p-catalyzed methylation can also modulate protein-protein interactions. Hmt1p is conserved from unicellular eukaryotes through to mammals where its ortholog, PRMT1, is lethal upon knockout. In yeast, however, the effect of knockout on the transcriptome and proteome has not been de  ...[more]

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