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Sci Rep. 2017 Sep 11;7(1):11063. doi: 10.1038/s41598-017-11296-9.

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

Author information

1
The ithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.
2
Proteomics Core Facility, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia.
3
The ithree institute, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia. Steven.Djordjevic@uts.edu.au.
4
Proteomics Core Facility, University of Technology Sydney, PO Box 123, Broadway, NSW, 2007, Australia. Steven.Djordjevic@uts.edu.au.

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.

PMID:
28894154
PMCID:
PMC5593965
DOI:
10.1038/s41598-017-11296-9
[Indexed for MEDLINE]
Free PMC Article

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