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Yeast methylarginine peptide IPS

ABSTRACT: Yeast peptides immunoprecipitated with an anti-mono-methylarginine antibody, analysis on Orbitrap Velos with ETD.

INSTRUMENT(S):

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

SUBMITTER: Daniel Yagoub

LAB HEAD: Professor Marc Wilkins

PROVIDER: PXD002151 | Pride | 2017-07-03

REPOSITORIES: Pride

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			Action	DRS
	DY_01_06-01-14mma-20-12-13_5ul.raw	Raw
	DY_15-03-13_IP-full.raw	Raw
	Daniel-12-06-12-mma.raw	Raw
	Daniel-29-05-12-mArgST-Eluate.raw	Raw
	Daniel_03-03-133_iIP-full-biginj1.raw	Raw

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1 - 5 of 21

Publications

Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively methylated and are substrates of the arginine methyltransferase Hmt1p.

Yagoub Daniel D Hart-Smith Gene G Moecking Jonas J Erce Melissa A MA Wilkins Marc R MR

Proteomics 20150810 18

The Hmt1 methyltransferase is the predominant arginine methyltransferase in Saccharomyces cerevisiae. There are 18 substrate proteins described for this methyltransferase, however native sites of methylation have only been identified on two of these proteins. Here we used peptide immunoaffinity enrichment, followed by LC-ETD-MS/MS, to discover 21 native sites of arginine methylation on five putative Hmt1 substrate proteins, namely Gar1p (H/ACA ribonucleoprotein complex subunit 1), Nop1p (rRNA 2' ...[more]

PMID: 26081071

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