A new protease to decipher the human proteome
The human proteome project (HPP), following on the heels of the human genome project, aims to describe every protein and their variants in us, so that we can understand the basis of disease.
To prepare protein samples for mass spectrometry analysis, proteins must first be cut into smaller pieces by proteases. Yet proteases that are currently available miss over 3,000 proteins, the so-called “missing proteins,” because they cannot detect the ends and certain modified parts of proteins that are very important for their functions in cell signalling.
A team of UBC LSI researchers led by Professor Christopher Overall has discovered a new protease they have called LysargiNase to prepare proteins for HPP analysis that shows enormous potential in discovering missing proteins, in particular the C-terminal ends and phosphorylation modified proteins. The study is published in Nature Methods.
Christopher Overall is a member of the LSI’s Centre for Blood Research (CBR) Group, Professor in the Department of Oral & Biological Medical Sciences, and Canada Research Chair in Metalloproteinase Proteomics & Systems Biology.
Huesgen et al., 2015. LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification. Nature Methods.