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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00006698naa a2200625 4500
001oai:DiVA.org:uu-434441
003SwePub
008210212s2020 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-4344412 URI
0247 a https://doi.org/10.1093/molbev/msaa1862 DOI
040 a (SwePub)uu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Emery-Corbin, Samantha J.u Walter & Eliza Hall Inst Med Res, Populat Hlth & Immun Div, Melbourne, Vic, Australia.;Univ Melbourne, Dept Med Biol, Parkville, Vic, Australia.4 aut
2451 0a Eukaryote-Conserved Methylarginine Is Absent in Diplomonads and Functionally Compensated in Giardia
264 c 2020-07-23
264 1b OXFORD UNIV PRESS,c 2020
338 a electronic2 rdacarrier
520 a 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 evidence for methylarginine absence in proteomes of Giardia but readily detect methyllysine. We bioinformatically infer 11 lysine-methyltransferases in Giardia, including highly diverged Su(var)3-9, Enhancer-of-zeste and Trithorax proteins with reduced domain architectures, and novel annotations demonstrating conserved methyllysine regulation of eukaryotic elongation factor 1 alpha. Using mass spectrometry, we identifymore than 200methyllysine sites in Giardia, including in species-specific gene families involved in cytoskeletal regulation, enriched in coiled-coil features. Finally, we use known methylation inhibitors to show that methylation plays key roles in replication and cyst formation in this parasite. This study highlights reduced methylation enzymes, sites, and functions early in eukaryote evolution, including absent methylarginine networks in the Diplomonadida. These results challenge the view that arginine methylation is eukaryote conserved and demonstrate that functional compensation of methylarginine was possible preceding expansion and diversification of these key networks in higher eukaryotes.
650 7a NATURVETENSKAPx Biologix Evolutionsbiologi0 (SwePub)106152 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Evolutionary Biology0 (SwePub)106152 hsv//eng
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653 a methylproteome
653 a methylarginine
653 a methyllysine
653 a Diplomonadida
653 a Metamonada
653 a Giardia
7001 a Hamey, Joshua J.u Univ New South Wales, Sch Biotechnol & Biomol Sci, Sydney, NSW, Australia.4 aut
7001 a Ansell, Brendan R. E.u Walter & Eliza Hall Inst Med Res, Populat Hlth & Immun Div, Melbourne, Vic, Australia.;Univ Melbourne, Dept Med Biol, Parkville, Vic, Australia.4 aut
7001 a Balan, Baluu Walter & Eliza Hall Inst Med Res, Populat Hlth & Immun Div, Melbourne, Vic, Australia.;Univ Melbourne, Dept Med Biol, Parkville, Vic, Australia.;Univ Melbourne, Fac Vet & Agr Sci, Melbourne Vet Sch, Dept Vet Biosci, Parkville, Vic, Australia.4 aut
7001 a Tichkule, Swapnilu Walter & Eliza Hall Inst Med Res, Populat Hlth & Immun Div, Melbourne, Vic, Australia.;Univ Melbourne, Dept Med Biol, Parkville, Vic, Australia.4 aut
7001 a Stroehlein, Andreas J.u Univ Melbourne, Fac Vet & Agr Sci, Melbourne Vet Sch, Dept Vet Biosci, Parkville, Vic, Australia.4 aut
7001 a Cooper, Crystalu Queensland Univ Technol, Inst Future Environm, Cent Analyt Res Facil CARF, Brisbane, Qld, Australia.4 aut
7001 a McInerney, Bernie, Vu Macquarie Univ, Australian Proteome Anal Facil APAF, N Ryde, NSW, Australia.4 aut
7001 a Hediyeh-Zadeh, Sorooru Univ Melbourne, Dept Med Biol, Parkville, Vic, Australia.;Walter & Eliza Hall Inst Med Res, Bioinformat Div, Parkville, Vic, Australia.4 aut
7001 a Vuong, Danielu Microbial Screening Technol, Smithfield, NSW, Australia.4 aut
7001 a Crombie, Andrewu Microbial Screening Technol, Smithfield, NSW, Australia.4 aut
7001 a Lacey, Ernestu Microbial Screening Technol, Smithfield, NSW, Australia.;Macquarie Univ, Fac Sci, Chem & Biomol Sci, N Ryde, NSW, Australia.4 aut
7001 a Davis, Melissa J.u Univ Melbourne, Dept Med Biol, Parkville, Vic, Australia.;Walter & Eliza Hall Inst Med Res, Bioinformat Div, Parkville, Vic, Australia.4 aut
7001 a Wilkins, Marc R.u Univ New South Wales, Sch Biotechnol & Biomol Sci, Sydney, NSW, Australia.4 aut
7001 a Bahlo, Melanieu Walter & Eliza Hall Inst Med Res, Populat Hlth & Immun Div, Melbourne, Vic, Australia.;Univ Melbourne, Dept Med Biol, Parkville, Vic, Australia.4 aut
7001 a Svärd, Staffanu Uppsala universitet,Mikrobiologi4 aut0 (Swepub:uu)stsva021
7001 a Gasser, Robin B.u Univ Melbourne, Fac Vet & Agr Sci, Melbourne Vet Sch, Dept Vet Biosci, Parkville, Vic, Australia.4 aut
7001 a Jex, Aaron R.u Walter & Eliza Hall Inst Med Res, Populat Hlth & Immun Div, Melbourne, Vic, Australia.;Univ Melbourne, Dept Med Biol, Parkville, Vic, Australia.;Univ Melbourne, Fac Vet & Agr Sci, Melbourne Vet Sch, Dept Vet Biosci, Parkville, Vic, Australia.4 aut
7102 a Walter & Eliza Hall Inst Med Res, Populat Hlth & Immun Div, Melbourne, Vic, Australia.;Univ Melbourne, Dept Med Biol, Parkville, Vic, Australia.b Univ New South Wales, Sch Biotechnol & Biomol Sci, Sydney, NSW, Australia.4 org
7730 t Molecular biology and evolutiond : OXFORD UNIV PRESSg 37:12, s. 3525-3549q 37:12<3525-3549x 0737-4038x 1537-1719
8564 u https://doi.org/10.1093/molbev/msaa186y Fulltext
8564 u https://uu.diva-portal.org/smash/get/diva2:1528086/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print
8564 u https://academic.oup.com/mbe/article-pdf/37/12/3525/34927425/msaa186.pdf
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-434441
8564 8u https://doi.org/10.1093/molbev/msaa186

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