Journal
NATURE METHODS
Volume 3, Issue 7, Pages 533-539Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NMETH891
Keywords
-
Categories
Funding
- NHLBI NIH HHS [N01-HV-28179] Funding Source: Medline
- NIGMS NIH HHS [GM060980, R01 GM060980, R01 GM060980-06A1] Funding Source: Medline
Ask authors/readers for more resources
Tandem mass spectrometry (MS/MS) allows for the rapid identification of many types of post-translational modifications (PTMs), especially those that can be detected by a diagnostic mass shift in one or more peptide fragment ions (for example, phosphorylation). But some PTMs (for example, SUMOs and other ubiquitin-like modifiers) themselves produce multiple fragment ions; combined with fragments from the modified target peptide, a complex overlapping fragmentation pattern is thus generated, which is uninterpretable by standard peptide sequencing software. Here we introduce SUMmOn, an automated pattern recognition tool that detects diagnostic PTM fragment ion series within complex MS/MS spectra, to identify modified peptides and modification sites within these peptides. Using SUMmOn, we demonstrate for the first time that human SUMO-1 multimerizes in vitro primarily via three N-terminal lysines, Lys7, Lys16 and Lys17. Notably, our method is theoretically applicable to any type of modification or chemical moiety generating a unique fragment ion pattern.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available