Hierarchical Rules for Argonaute Loading in Drosophila
Drosophila Argonaute-1 and Argonaute-2 differ in function and small RNA content. AGO2 binds to siRNAs, whereas AGO1 is almost exclusively occupied by microRNAs. MicroRNA duplexes are intrinsically asymmetric, with one strand, the miR strand, preferentially entering AGO1 to recognize and regulate the...
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| Published in | Molecular cell Vol. 36; no. 3; pp. 445 - 456 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
13.11.2009
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Drosophila Argonaute-1 and Argonaute-2 differ in function and small RNA content. AGO2 binds to siRNAs, whereas AGO1 is almost exclusively occupied by microRNAs. MicroRNA duplexes are intrinsically asymmetric, with one strand, the miR strand, preferentially entering AGO1 to recognize and regulate the expression of target mRNAs. The other strand, miR∗, has been viewed as a byproduct of microRNA biogenesis. Here, we show that miR∗s are often loaded as functional species into AGO2. This indicates that each microRNA precursor can potentially produce two mature small RNA strands that are differentially sorted within the RNAi pathway. miR∗ biogenesis depends upon the canonical microRNA pathway, but loading into AGO2 is mediated by factors traditionally dedicated to siRNAs. By inferring and validating hierarchical rules that predict differential AGO loading, we find that intrinsic determinants, including structural and thermodynamic properties of the processed duplex, regulate the fate of each RNA strand within the RNAi pathway. |
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| AbstractList | Drosophila
Argonaute-1 and Argonaute-2 differ in function and small RNA content. AGO2 binds to siRNAs, whereas AGO1 is almost exclusively occupied by microRNAs. MicroRNA duplexes are intrinsically asymmetric, with one strand, the miR strand, preferentially entering AGO1 to recognize and regulate the expression of target mRNAs. The other strand, miR*, has been viewed as a byproduct of microRNA biogenesis. Here, we show that miR*s are often loaded as functional species into AGO2. This indicates that each microRNA precursor can potentially produce two mature small RNA strands that are differentially sorted within the RNAi pathway. miR* biogenesis depends upon the canonical microRNA pathway, but loading into AGO2 is mediated by factors traditionally dedicated to siRNAs. By inferring and validating hierarchical rules that predict differential AGO loading, we find that intrinsic determinants, including structural and thermodynamic properties of the processed duplex, regulate the fate of each RNA strand within the RNAi pathway. Drosophila Argonaute-1 and Argonaute-2 differ in function and small RNA content. AGO2 binds to siRNAs, whereas AGO1 is almost exclusively occupied by microRNAs. MicroRNA duplexes are intrinsically asymmetric, with one strand, the miR strand, preferentially entering AGO1 to recognize and regulate the expression of target mRNAs. The other strand, miR*, has been viewed as a byproduct of microRNA biogenesis. Here, we show that miR*s are often loaded as functional species into AGO2. This indicates that each microRNA precursor can potentially produce two mature small RNA strands that are differentially sorted within the RNAi pathway. miR* biogenesis depends upon the canonical microRNA pathway, but loading into AGO2 is mediated by factors traditionally dedicated to siRNAs. By inferring and validating hierarchical rules that predict differential AGO loading, we find that intrinsic determinants, including structural and thermodynamic properties of the processed duplex, regulate the fate of each RNA strand within the RNAi pathway. Drosophila Argonaute-1 and Argonaute-2 differ in function and small RNA content. AGO2 binds to siRNAs, whereas AGO1 is almost exclusively occupied by microRNAs. MicroRNA duplexes are intrinsically asymmetric, with one strand, the miR strand, preferentially entering AGO1 to recognize and regulate the expression of target mRNAs. The other strand, miR∗, has been viewed as a byproduct of microRNA biogenesis. Here, we show that miR∗s are often loaded as functional species into AGO2. This indicates that each microRNA precursor can potentially produce two mature small RNA strands that are differentially sorted within the RNAi pathway. miR∗ biogenesis depends upon the canonical microRNA pathway, but loading into AGO2 is mediated by factors traditionally dedicated to siRNAs. By inferring and validating hierarchical rules that predict differential AGO loading, we find that intrinsic determinants, including structural and thermodynamic properties of the processed duplex, regulate the fate of each RNA strand within the RNAi pathway. Drosophila Argonaute-1 and Argonaute-2 differ in function and small RNA content. AGO2 binds to siRNAs, whereas AGO1 is almost exclusively occupied by microRNAs. MicroRNA duplexes are intrinsically asymmetric, with one strand, the miR strand, preferentially entering AGO1 to recognize and regulate the expression of target mRNAs. The other strand, miR[super], has been viewed as a byproduct of microRNA biogenesis. Here, we show that miR[super]*s are often loaded as functional species into AGO2. This indicates that each microRNA precursor can potentially produce two mature small RNA strands that are differentially sorted within the RNAi pathway. miR[super]* biogenesis depends upon the canonical microRNA pathway, but loading into AGO2 is mediated by factors traditionally dedicated to siRNAs. By inferring and validating hierarchical rules that predict differential AGO loading, we find that intrinsic determinants, including structural and thermodynamic properties of the processed duplex, regulate the fate of each RNA strand within the RNAi pathway. |
| Author | Villalta, Christians Gordon, Assaf Hannon, Gregory J. Zhou, Rui Czech, Benjamin Binari, Richard Erlich, Yaniv Perrimon, Norbert Brennecke, Julius |
| AuthorAffiliation | 1 Watson School of Biological Sciences Howard Hughes Medical Institute Cold Spring Harbor Laboratory 1 Bungtown Road Cold Spring Harbor, NY 11724, USA 2 Harvard Medical School Department of Genetics Howard Hughes Medical Institute 77 Avenue Louis Pasteur Boston, MA 02115, USA |
| AuthorAffiliation_xml | – name: 1 Watson School of Biological Sciences Howard Hughes Medical Institute Cold Spring Harbor Laboratory 1 Bungtown Road Cold Spring Harbor, NY 11724, USA – name: 2 Harvard Medical School Department of Genetics Howard Hughes Medical Institute 77 Avenue Louis Pasteur Boston, MA 02115, USA |
| Author_xml | – sequence: 1 givenname: Benjamin surname: Czech fullname: Czech, Benjamin organization: Watson School of Biological Sciences, Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA – sequence: 2 givenname: Rui surname: Zhou fullname: Zhou, Rui organization: Department of Genetics, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA – sequence: 3 givenname: Yaniv surname: Erlich fullname: Erlich, Yaniv organization: Watson School of Biological Sciences, Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA – sequence: 4 givenname: Julius surname: Brennecke fullname: Brennecke, Julius organization: Watson School of Biological Sciences, Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA – sequence: 5 givenname: Richard surname: Binari fullname: Binari, Richard organization: Department of Genetics, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA – sequence: 6 givenname: Christians surname: Villalta fullname: Villalta, Christians organization: Department of Genetics, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA – sequence: 7 givenname: Assaf surname: Gordon fullname: Gordon, Assaf organization: Watson School of Biological Sciences, Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA – sequence: 8 givenname: Norbert surname: Perrimon fullname: Perrimon, Norbert email: perrimon@receptor.med.harvard.edu organization: Department of Genetics, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA – sequence: 9 givenname: Gregory J. surname: Hannon fullname: Hannon, Gregory J. email: hannon@cshl.edu organization: Watson School of Biological Sciences, Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19917252$$D View this record in MEDLINE/PubMed |
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| Snippet | Drosophila Argonaute-1 and Argonaute-2 differ in function and small RNA content. AGO2 binds to siRNAs, whereas AGO1 is almost exclusively occupied by... Drosophila Argonaute-1 and Argonaute-2 differ in function and small RNA content. AGO2 binds to siRNAs, whereas AGO1 is almost exclusively occupied by... |
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| SubjectTerms | 3' Untranslated Regions Animals Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Argonaute 2 protein Argonaute Proteins Base Pairing Blotting, Northern Cell Line Drosophila Drosophila melanogaster - cytology Drosophila melanogaster - genetics Drosophila melanogaster - metabolism Drosophila Proteins - genetics Drosophila Proteins - metabolism Gene expression Immunoprecipitation MicroRNAs - chemistry MicroRNAs - genetics MicroRNAs - metabolism miRNA Models, Biological mRNA Nucleic Acid Conformation Protein Binding PROTEINS RNA RNA Interference RNA Precursors - genetics RNA Precursors - metabolism RNA, Double-Stranded - genetics RNA, Double-Stranded - metabolism RNA, Messenger - genetics RNA, Messenger - metabolism RNA, Small Interfering - chemistry RNA, Small Interfering - genetics RNA, Small Interfering - metabolism RNA-Induced Silencing Complex - genetics RNA-Induced Silencing Complex - metabolism RNA-mediated interference siRNA Thermodynamics |
| Title | Hierarchical Rules for Argonaute Loading in Drosophila |
| URI | https://dx.doi.org/10.1016/j.molcel.2009.09.028 https://www.ncbi.nlm.nih.gov/pubmed/19917252 https://search.proquest.com/docview/1028077956 https://search.proquest.com/docview/733524852 https://pubmed.ncbi.nlm.nih.gov/PMC2795325 |
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