{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7(1)"],"submitter":["Berry IJ"],"pubmed_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. Glyceralde"],"journal":["Scientific reports"],"pagination":["11063"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5593965"],"repository":["biostudies-literature"],"pubmed_title":["N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen."],"pmcid":["PMC5593965"],"pubmed_authors":["Berry IJ","Raymond BBA","Padula MP","Widjaja M","Djordjevic SP","Jarocki VM","Tacchi JL"],"additional_accession":[]},"is_claimable":false,"name":"N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen.","description":"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. Glyceralde","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Sep","modification":"2026-05-01T08:03:58.765Z","creation":"2025-05-29T21:55:49.833Z"},"accession":"S-EPMC5593965","cross_references":{"pubmed":["28894154"],"doi":["10.1038/s41598-017-11296-9"]}}