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dc.contributor.authorAmeres, Stefan L.
dc.contributor.authorHung, Jui-Hung
dc.contributor.authorXu, Jia
dc.contributor.authorWeng, Zhiping
dc.contributor.authorZamore, Phillip D.
dc.date2022-08-11T08:07:59.000
dc.date.accessioned2022-08-23T15:38:16Z
dc.date.available2022-08-23T15:38:16Z
dc.date.issued2011-01-01
dc.date.submitted2013-06-27
dc.identifier.citationRNA. 2011 Jan;17(1):54-63. doi: 10.1261/rna.2498411. <a href="http://dx.doi.org/10.1261/rna.2498411" target="_blank">Link to article on publisher's site</a>
dc.identifier.issn1469-9001
dc.identifier.doi10.1261/rna.2498411
dc.identifier.pmid21106652
dc.identifier.urihttp://hdl.handle.net/20.500.14038/25901
dc.description.abstractIn flies, 22-23-nucleotide (nt) microRNA duplexes typically contain mismatches and begin with uridine, so they bind Argonaute1 (Ago1), whereas 21-nt siRNA duplexes are perfectly paired and begin with cytidine, promoting their loading into Ago2. A subset of Drosophila endogenous siRNAs-the hairpin-derived hp-esiRNAs-are born as mismatched duplexes that often begin with uridine. These would be predicted to load into Ago1, yet accumulate at steady-state bound to Ago2. In vitro, such hp-esiRNA duplexes assemble into Ago1. In vivo, they encounter complementary target mRNAs that trigger their tailing and trimming, causing Ago1-loaded hp-esiRNAs to be degraded. In contrast, Ago2-associated hp-esiRNAs are 2'-O-methyl modified at their 3' ends, protecting them from tailing and trimming. Consequently, the steady-state distribution of esiRNAs reflects not only their initial sorting between Ago1 and Ago2 according to their duplex structure, length, and first nucleotide, but also the targeted destruction of the single-stranded small RNAs after their loading into an Argonaute protein.
dc.language.isoen_US
dc.publisherCold Spring Harbor Laboratory Press
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=21106652&dopt=Abstract">Link to article in PubMed</a>
dc.rightsFreely available online through the RNA Open Access option. This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genome.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported License), as described at http://creativecommons.org/licenses/by-nc/3.0/.
dc.subjectAnimals
dc.subjectArgonaute Proteins
dc.subjectBase Pairing
dc.subjectBase Sequence
dc.subjectCross-Linking Reagents
dc.subjectDrosophila Proteins
dc.subjectDrosophila melanogaster
dc.subjectEukaryotic Initiation Factors
dc.subjectImmunoprecipitation
dc.subjectMicroRNAs
dc.subjectMolecular Sequence Data
dc.subjectProtein Binding
dc.subjectRNA
dc.subjectRNA, Messenger
dc.subjectRNA, Small Interfering
dc.subjectRNA-Induced Silencing Complex
dc.subjectBioinformatics
dc.subjectComputational Biology
dc.subjectGenetics and Genomics
dc.subjectMolecular Biology
dc.subjectSystems Biology
dc.titleTarget RNA-directed tailing and trimming purifies the sorting of endo-siRNAs between the two Drosophila Argonaute proteins
dc.typeArticle
dc.source.journaltitleRNA (New York, N.Y.)
dc.source.volume17
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1048&amp;context=bioinformatics_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/bioinformatics_pubs/43
dc.identifier.contextkey4262491
refterms.dateFOA2022-08-23T15:38:16Z
html.description.abstract<p>In flies, 22-23-nucleotide (nt) microRNA duplexes typically contain mismatches and begin with uridine, so they bind Argonaute1 (Ago1), whereas 21-nt siRNA duplexes are perfectly paired and begin with cytidine, promoting their loading into Ago2. A subset of Drosophila endogenous siRNAs-the hairpin-derived hp-esiRNAs-are born as mismatched duplexes that often begin with uridine. These would be predicted to load into Ago1, yet accumulate at steady-state bound to Ago2. In vitro, such hp-esiRNA duplexes assemble into Ago1. In vivo, they encounter complementary target mRNAs that trigger their tailing and trimming, causing Ago1-loaded hp-esiRNAs to be degraded. In contrast, Ago2-associated hp-esiRNAs are 2'-O-methyl modified at their 3' ends, protecting them from tailing and trimming. Consequently, the steady-state distribution of esiRNAs reflects not only their initial sorting between Ago1 and Ago2 according to their duplex structure, length, and first nucleotide, but also the targeted destruction of the single-stranded small RNAs after their loading into an Argonaute protein.</p>
dc.identifier.submissionpathbioinformatics_pubs/43
dc.contributor.departmentProgram in Bioinformatics and Integrative Biology
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages54-63


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