Proteomics

Dataset Information

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MT-MAMS: protein methyltransferase motif analysis by mass spectrometry


ABSTRACT: Protein methyltransferases can recognise their substrates through linear sequence motifs and determination of these motifs is critical to understand methyltransferase mechanism, function and drug targeting. Here we describe MT-MAMS (methyltransferase motif analysis by mass spectrometry), a quantitative approach to characterise methyltransferase substrate recognition motifs and enzyme processivity. We validated MT-MAMS by application to lysine methyltransferase G9a, then determined the recognition motifs of Efm1 and major arginine methyltransferases Hmt1 and PRMT1.

INSTRUMENT(S): Orbitrap Fusion Lumos, LTQ Orbitrap Velos, Q Exactive

ORGANISM(S): Homo Sapiens (human) Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Joshua Hamey  

LAB HEAD: Marc R Wilkins

PROVIDER: PXD009515 | Pride | 2018-09-03

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Datamanuallyanalysed.txt Txt
EF1A-ve_metassay_lysarg_1ul.dat Other
EF1A-ve_metassay_lysarg_1ul.mgf Mgf
EF1A-ve_metassay_lysarg_1ul.raw Raw
EF1A-ve_metassay_tryp_1ul.dat Other
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Publications

MT-MAMS: Protein Methyltransferase Motif Analysis by Mass Spectrometry.

Hamey Joshua J JJ   Separovich Ryan J RJ   Wilkins Marc R MR  

Journal of proteome research 20180906 10


Protein methyltransferases often recognize their substrates through linear sequence motifs. The determination of these motifs is critical to understand methyltransferase mechanism, function, and drug targeting. Here we describe MT-MAMS (methyltransferase motif analysis by mass spectrometry), a quantitative approach to characterize methyltransferase substrate recognition motifs. In MT-MAMS, peptide sets are synthesized which contain all amino acid substitutions at single positions within a templa  ...[more]

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