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Analysis of the ubiquitinated peptides using the yeast Rpt2-normal, G2A and G2delta strains

ABSTRACT: Ubiquitinated peptides (KGG peptides) purified from the yeast strains with or without mutation on the N-myristoylation site of the proteasome Rpt2 subunit were analyzed by an LTQ-Orbitrap Velos. The MS data was analyzed by the Progenesis LC-MS software.

INSTRUMENT(S): LTQ Orbitrap Velos

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

SUBMITTER: Ayuko Kimura

LAB HEAD: Hisashi Hirano

PROVIDER: PXD002274 | Pride | 2017-08-25

REPOSITORIES: Pride

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			Action	DRS
	150119_Ub-Del-1.raw	Raw
	150119_Ub-Del-2.raw	Raw
	150119_Ub-Del-3.raw	Raw
	150119_Ub-Mut-1.raw	Raw
	150119_Ub-Mut-2.raw	Raw

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Publications

N-Myristoylation of the Rpt2 subunit of the yeast 26S proteasome is implicated in the subcellular compartment-specific protein quality control system.

Kimura Ayuko A Kurata Yoichi Y Nakabayashi Jun J Kagawa Hiroyuki H Hirano Hisashi H

Journal of proteomics 20150904

Ubiquitination is the posttranslational modification of a protein by covalent attachment of ubiquitin. Controlled proteolysis via the ubiquitin-proteasome system (\UPS) alleviates cellular stress by clearing misfolded proteins. In budding yeast, UPS within the nucleus degrades the nuclear proteins as well as proteins imported from the cytoplasm. While the predominantly nuclear localization of the yeast proteasome is maintained by the importin-mediated transport, N-myristoylation of the proteasom ...[more]

PMID: 26344132

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