Journal article

Eukaryote-ConservedMethylarginine Is Absent in Diplomonads and Functionally Compensated in Giardia

Samantha J Emery-Corbin, Joshua J Hamey, Brendan RE Ansell, Balu Balan, Swapnil Tichkule, Andreas J Stroehlein, Crystal Cooper, Bernie McInerney, Soroor Hediyeh-Zadeh, Daniel Vuong, Andrew Crombie, Ernest Lacey, Melissa J Davis, Marc R Wilkins, Melanie Bahlo, Staffan G Svard, Robin B Gasser, Aaron R Jex



Methylation is a common posttranslational modification of arginine and lysine in eukaryotic proteins. Methylproteomes are best characterized for higher eukaryotes, where they are functionally expanded and evolved complex regulation. However, this is not the case for protist species evolved from the earliest eukaryotic lineages. Here, we integrated bioinformatic, proteomic, and drug-screening data sets to comprehensively explore the methylproteome of Giardia duodenalis-a deeply branching parasitic protist. We demonstrate that Giardia and related diplomonads lack arginine-methyltransferases and have remodeled conserved RGG/RG motifs targeted by these enzymes. We also provide experimental evide..

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Awarded by Jack Brockhoff Foundation

Awarded by NHMRC

Awarded by Early Career NHMRC Fellowship

Funding Acknowledgements

This work, including the efforts of S.J.E.-C., was funded by a Jack Brockhoff Foundation Early Career (Grant No. JBF 4184, 2016). S.J.E.-C., B.R.E.A., B.B., S.T., S.H.Z., M.B., M.J.D., and A.R.J. are supported by the Victorian State Government Operational Infrastructure Support and Australian Government National Health and Medical Research Council Independent Research Institute Infrastructure Support Scheme. A.R.J. is also supported by an NHMRC Career Development Fellowship (APP1126395). M.B. is supported by an NHMRC Senior Research Fellowship (1102971). B.R.E.A. is supported by an Early Career NHMRC Fellowship (APP1157776). The authors acknowledge the facilities and the scientific and technical assistance supported by Microscopy Australia (MA) at the Central Analytical Research Facility (CARF), Institute for Future Environments, Queensland University of Technology, Brisbane, Australia. The authors also acknowledge the Melbourne Mass Spectrometry and Proteomics Facility of the Bio21 Molecular Science and Biotechnology Institute at the University of Melbourne, including Shuai Nie, Ching-seng Ang, and Nick Williamson, for the support of MS analysis. The authors also acknowledge the NCRIS-enabled facilities of the Australian Proteome Analysis Facility (APAF) of Macquarie University, Sydney. The authors acknowledge the facilities and staff of the Bioanalytical Mass Spectrometry Facility at the University of New South Wales.