What is it about?
We use dimethyl labelling and mass spectrometry to identify Mycoplasma hyopneumoniae (a genome-reduced important pig pathogen) proteins that have been proteolytically processed. We found that the proteins that were cut up the most, had a greater binding affinity to a range of host proteins, suggesting that cleavage changes a protein's structure to expose more protein interaction sites. We also found novel N-terminal methionine excision in some proteins and discovered that not methionine aminopeptidase (the protease typically responsible), but two previously characterised multifunctional proteases were involved.
Featured Image
Why is it important?
Genome-reduced organisms "do more with less". Here we show that through proteolytic processing, Mycoplasma hyopneumoniae can expand its proteins functions.
Perspectives
This paper I co-authored with Iain. I enjoyed assisting in analysing the data his N-terminomic study generated and finding a potential candidate for the extensive proteolytic activity found.
Dr Veronica M Jarocki
University of Technology Sydney
Read the Original
This page is a summary of: N-terminomics identifies widespread endoproteolysis and novel methionine excision in a genome-reduced bacterial pathogen, Scientific Reports, September 2017, Nature,
DOI: 10.1038/s41598-017-11296-9.
You can read the full text:
Contributors
The following have contributed to this page
