Natural Variation of the Amino-Terminal Glutamine-Rich Domain in Drosophila Argonaute2 Is Not Associated with Developmental Defects

Hain, D; Bettencourt, BR; Okamura, K; Csorba, T; Meyer, W; Jin, Z; Biggerstaff, J; Siomi, H; Hutvagner, G; Lai, EC; Welte, M; Müller, HAJ

Natural Variation of the Amino-Terminal Glutamine-Rich Domain in Drosophila Argonaute2 Is Not Associated with Developmental Defects

Hain, D Bettencourt, BR Okamura, K Csorba, T Meyer, W Jin, Z Biggerstaff, J Siomi, H Hutvagner, G

Lai, EC Welte, M Müller, HAJ

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Publication Type:: Journal Article
Citation:: PLoS ONE, 2010, 5 (12), pp. 1 - 14
Issue Date:: 2010-12-01

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Field	Value	Language
dc.contributor.author	Hain, D	en_US
dc.contributor.author	Bettencourt, BR	en_US
dc.contributor.author	Okamura, K	en_US
dc.contributor.author	Csorba, T	en_US
dc.contributor.author	Meyer, W	en_US
dc.contributor.author	Jin, Z	en_US
dc.contributor.author	Biggerstaff, J	en_US
dc.contributor.author	Siomi, H	en_US
dc.contributor.author	Hutvagner, G https://orcid.org/0000-0002-7231-9446	en_US
dc.contributor.author	Lai, EC	en_US
dc.contributor.author	Welte, M	en_US
dc.contributor.author	Müller, HAJ	en_US
dc.date.available	2010-11-08	en_US
dc.date.issued	2010-12-01	en_US
dc.identifier.citation	PLoS ONE, 2010, 5 (12), pp. 1 - 14	en_US
dc.identifier.uri	http://hdl.handle.net/10453/15381
dc.description.abstract	The Drosophila argonaute2 (ago2) gene plays a major role in siRNA mediated RNA silencing pathways. Unlike mammalian Argonaute proteins, the Drosophila protein has an unusual amino-terminal domain made up largely of multiple copies of glutamine-rich repeats (GRRs). We report here that the ago2 locus produces an alternative transcript that encodes a putative short isoform without this amino-terminal domain. Several ago2 mutations previously reported to be null alleles only abolish expression of the long, GRR-containing isoform. Analysis of drop out (dop) mutations had previously suggested that variations in GRR copy number result in defects in RNAi and embryonic development. However, we find that dop mutations genetically complement transcript-null alleles of ago2 and that ago2 alleles with variant GRR copy numbers support normal development. In addition, we show that the assembly of the central RNAi machinery, the RISC (RNA induced silencing complex), is unimpaired in embryos when GRR copy number is altered. In fact, we find that GRR copy number is highly variable in natural D. melanogaster populations as well as in laboratory strains. Finally, while many other insects share an extensive, glutamine-rich Ago2 amino-terminal domain, its primary sequence varies drastically between species. Our data indicate that GRR variation does not modulate an essential function of Ago2 and that the amino-terminal domain of Ago2 is subject to rapid evolution. © 2010 Hain et al.	en_US
dc.relation.ispartof	PLoS ONE	en_US
dc.relation.isbasedon	10.1371/journal.pone.0015264	en_US
dc.subject.classification	General Science & Technology	en_US
dc.subject.mesh	Animals	en_US
dc.subject.mesh	RNA-Induced Silencing Complex	en_US
dc.subject.mesh	Glutamine	en_US
dc.subject.mesh	Drosophila Proteins	en_US
dc.subject.mesh	Protein Isoforms	en_US
dc.subject.mesh	Phylogeny	en_US
dc.subject.mesh	Gene Expression Regulation, Developmental	en_US
dc.subject.mesh	Gene Silencing	en_US
dc.subject.mesh	RNA Interference	en_US
dc.subject.mesh	Protein Structure, Tertiary	en_US
dc.subject.mesh	Gene Dosage	en_US
dc.subject.mesh	Heterozygote	en_US
dc.subject.mesh	Mutation	en_US
dc.subject.mesh	Alleles	en_US
dc.subject.mesh	Female	en_US
dc.subject.mesh	Genetic Variation	en_US
dc.subject.mesh	Argonaute Proteins	en_US
dc.title	Natural Variation of the Amino-Terminal Glutamine-Rich Domain in Drosophila Argonaute2 Is Not Associated with Developmental Defects	en_US
dc.type	Journal Article
utslib.citation.volume	12	en_US
utslib.citation.volume	5	en_US
utslib.for	0903 Biomedical Engineering	en_US
dc.location.activity	ISI:000285381200020	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology
pubs.organisational-group	/University of Technology Sydney/Faculty of Engineering and Information Technology/School of Biomedical Engineering
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
utslib.copyright.status	open_access
pubs.issue	12	en_US
pubs.publication-status	Published	en_US
pubs.volume	5	en_US

Abstract:

The Drosophila argonaute2 (ago2) gene plays a major role in siRNA mediated RNA silencing pathways. Unlike mammalian Argonaute proteins, the Drosophila protein has an unusual amino-terminal domain made up largely of multiple copies of glutamine-rich repeats (GRRs). We report here that the ago2 locus produces an alternative transcript that encodes a putative short isoform without this amino-terminal domain. Several ago2 mutations previously reported to be null alleles only abolish expression of the long, GRR-containing isoform. Analysis of drop out (dop) mutations had previously suggested that variations in GRR copy number result in defects in RNAi and embryonic development. However, we find that dop mutations genetically complement transcript-null alleles of ago2 and that ago2 alleles with variant GRR copy numbers support normal development. In addition, we show that the assembly of the central RNAi machinery, the RISC (RNA induced silencing complex), is unimpaired in embryos when GRR copy number is altered. In fact, we find that GRR copy number is highly variable in natural D. melanogaster populations as well as in laboratory strains. Finally, while many other insects share an extensive, glutamine-rich Ago2 amino-terminal domain, its primary sequence varies drastically between species. Our data indicate that GRR variation does not modulate an essential function of Ago2 and that the amino-terminal domain of Ago2 is subject to rapid evolution. © 2010 Hain et al.

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http://hdl.handle.net/10453/15381