N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-12

AUTHORS

Iain J. Berry, Veronica M. Jarocki, Jessica L. Tacchi, Benjamin B. A. Raymond, Michael Widjaja, Matthew P. Padula, Steven P. Djordjevic

ABSTRACT

Proteolytic processing alters protein function. Here we present the first systems-wide analysis of endoproteolysis in the genome-reduced pathogen Mycoplasma hyopneumoniae. 669 N-terminal peptides from 164 proteins were identified, demonstrating that functionally diverse proteins are processed, more than half of which 75 (53%) were accessible on the cell surface. Multiple cleavage sites were characterised, but cleavage with arginine in P1 predominated. Putative functions for a subset of cleaved fragments were assigned by affinity chromatography using heparin, actin, plasminogen and fibronectin as bait. Binding affinity was correlated with the number of cleavages in a protein, indicating that novel binding motifs are exposed, and protein disorder increases, after a cleavage event. Glyceraldehyde 3-phosphate dehydrogenase was used as a model protein to demonstrate this. We define the rules governing methionine excision, show that several aminopeptidases are involved, and propose that through processing, genome-reduced organisms can expand protein function. More... »

PAGES

11063

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41598-017-11296-9

DOI

http://dx.doi.org/10.1038/s41598-017-11296-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1091537379

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28894154


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