RT Journal Article
SR Electronic
T1 Global profiling of myristoylation in <em>Toxoplasma gondii</em> reveals key roles for lipidation in CDPK1 and MIC7 function
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 719062
DO 10.1101/719062
A1 Malgorzata Broncel
A1 Caia Dominicus
A1 Alexander Hunt
A1 Bethan Wallbank
A1 Stefania Federico
A1 Joanna Young
A1 Moritz Treeck
YR 2019
UL http://biorxiv.org/content/early/2019/07/30/719062.abstract
AB N-myristoylation is a ubiquitous class of protein lipidation across eukaryotes and N-myristoyl transferase has been proposed as an attractive drug target in several pathogens. Functionally the myristate often primes for subsequent palmitoylation and stable membrane attachment, however, growing evidence also suggests additional regulatory roles for myristoylation on proteins. Here we describe the first global chemoproteomic screening of protein myristoylation in Toxoplasma gondii. Through quantitative mass spectrometry coupled with validated chemoproteomic tools, we identify 65 myristoylated proteins. We report functionally important myristoylation on the key signalling protein CDPK1 and, surprisingly, myristoylation of the microneme protein 7 (MIC7), a predicted type-I-transmembrane protein. We demonstrate that myristoylation of MIC7 is not important for the trafficking to micronemes, but appears to play a role in host cell invasion. This dataset represents a large fraction of the parasite’s myristoylated proteome and a prerequisite to investigate this modification in Toxoplasma.