Proteomics

Dataset Information

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Yeast deletion Pdr5, Hsp42, Btn2 proteomics

ABSTRACT: In depth quantitative proteomics analysis of yeast deletion mutants of Pdr5, Hsp42, and Btn2 using TMT-MS3 on an Orbitrap Fusion.

INSTRUMENT(S): LTQ Orbitrap Elite

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

SUBMITTER: Christopher Hughes  

LAB HEAD: Gregg Morin

PROVIDER: PXD004459 | Pride | 2017-09-29

REPOSITORIES: pride

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Dataset's files

Source:
Action DRS
ch_26Nov2015_VeenaM_Yeast_TMT10_HpH_rep1a_-01_PSMs.txt Txt
ch_26Nov2015_VeenaM_Yeast_TMT10_HpH_rep1a_-01_Proteins.txt Txt
ch_26Nov2015_VeenaM_Yeast_TMT10_HpH_rep1a_1.raw Raw
ch_26Nov2015_VeenaM_Yeast_TMT10_HpH_rep1a_10.raw Raw
ch_26Nov2015_VeenaM_Yeast_TMT10_HpH_rep1a_11.raw Raw
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Publications

Selective aggregation of the splicing factor Hsh155 suppresses splicing upon genotoxic stress.

Mathew Veena V   Tam Annie S AS   Milbury Karissa L KL   Hofmann Analise K AK   Hughes Christopher S CS   Morin Gregg B GB   Loewen Christopher J R CJR   Stirling Peter C PC  

The Journal of cell biology 20171004 12

Upon genotoxic stress, dynamic relocalization events control DNA repair as well as alterations of the transcriptome and proteome, enabling stress recovery. How these events may influence one another is only partly known. Beginning with a cytological screen of genome stability proteins, we find that the splicing factor Hsh155 disassembles from its partners and localizes to both intranuclear and cytoplasmic protein quality control (PQC) aggregates under alkylation stress. Aggregate sequestration o  ...[more]

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