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Poster Presentations
Day 4, June 25（Wed.）
Room P (Maesato East, Foyer, Ocean Wing)
- 4P-AM-12
Expanded proteomics in the case of data-driven post-translational modification analysis
(RIKEN CSRSCSRS)
oNaoshi Dohmae
Proteomics is the largest data-volume application of mass spectrometry. We have developed an approach to expand the proteome by re-analysing proteomics data. One of these approaches is the proteogenomics approach, which focuses on open reading frames (ORFs) that are not genuine open reading frames (ORFs) of messenger RNA and attempts to discover new proteins by creating an ORF database that generates SEPs (short-ORF encoded peptides). We discovered and reported an overlapping ORF, oSCRIB, that suppresses the expression of the SCRIB gene. Next, we conducted a data-driven analysis that re-searched an existing database with special modifications, and discovered new lysine long-chain acylations by searching for palmitoylation and myristoylation, which are long-chain acyl groups that bind to lysine (2). In this study, we discovered new fucose modification sites in serum proteome data.
The enzymes that perform fucose modification are known to be protein O-glycosyltransferase 1 (POGLUT1), POFUT1 and -2, and POFUT2, and the consensus sequences are reported to be CXXXX(S/T)C and CX2-3(S/T)C, and many candidate modification sites have been reported.
We discovered a new fucosylation site using data-oriented analysis, but it was very unique in that it did not have the conventional consensus sequence.