Multilayer checkpoints for microRNA authenticity during RISC assembly
MicroRNAs (miRNAs) function through the RNA‐induced silencing complex (RISC), which contains an Argonaute (Ago) protein at the core. RISC assembly follows a two‐step pathway: miRNA/miRNA* duplex loading into Ago, and separation of the two strands within Ago. Here we show that the 5′ phosphate of the...
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| Published in | EMBO reports Vol. 12; no. 9; pp. 944 - 949 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
01.09.2011
Blackwell Publishing Ltd Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
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| Abstract | MicroRNAs (miRNAs) function through the RNA‐induced silencing complex (RISC), which contains an Argonaute (Ago) protein at the core. RISC assembly follows a two‐step pathway: miRNA/miRNA* duplex loading into Ago, and separation of the two strands within Ago. Here we show that the 5′ phosphate of the miRNA strand is essential for duplex loading into Ago, whereas the preferred 5′ nucleotide of the miRNA strand and the base‐pairing status in the seed region and the middle of the 3′ region function as additive anchors to Ago. Consequently, the miRNA authenticity is inspected at multiple steps during RISC assembly.
MicroRNAs are loaded into the RISC complex in order to exert their gene‐silencing activity. The authors show that microRNA authenticity is checked at multiple steps during RISC assembly. |
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| AbstractList | MicroRNAs (miRNAs) function through the RNA-induced silencing complex (RISC), which contains an Argonaute (Ago) protein at the core. RISC assembly follows a two-step pathway: miRNA/miRNA* duplex loading into Ago, and separation of the two strands within Ago. Here we show that the 5' phosphate of the miRNA strand is essential for duplex loading into Ago, whereas the preferred 5' nucleotide of the miRNA strand and the base-pairing status in the seed region and the middle of the 3' region function as additive anchors to Ago. Consequently, the miRNA authenticity is inspected at multiple steps during RISC assembly. MicroRNAs are loaded into the RISC complex in order to exert their gene-silencing activity. The authors show that microRNA authenticity is checked at multiple steps during RISC assembly. MicroRNAs (miRNAs) function through the RNA-induced silencing complex (RISC), which contains an Argonaute (Ago) protein at the core. RISC assembly follows a two-step pathway: miRNA/miRNA * duplex loading into Ago, and separation of the two strands within Ago. Here we show that the 5′ phosphate of the miRNA strand is essential for duplex loading into Ago, whereas the preferred 5′ nucleotide of the miRNA strand and the base-pairing status in the seed region and the middle of the 3′ region function as additive anchors to Ago. Consequently, the miRNA authenticity is inspected at multiple steps during RISC assembly. MicroRNAs (miRNAs) function through the RNA-induced silencing complex (RISC), which contains an Argonaute (Ago) protein at the core. RISC assembly follows a two-step pathway: miRNA/ miRNA* duplex loading into Ago, and separation of the two strands within Ago. Here we show that the 50 phosphate of the miRNA strand is essential for duplex loading into Ago, whereas the preferred 50 nucleotide of the miRNA strand and the base-pairing status in the seed region and the middle of the 30 region function as additive anchors to Ago. MicroRNAs (miRNAs) function through the RNA‐induced silencing complex (RISC), which contains an Argonaute (Ago) protein at the core. RISC assembly follows a two‐step pathway: miRNA/miRNA* duplex loading into Ago, and separation of the two strands within Ago. Here we show that the 5′ phosphate of the miRNA strand is essential for duplex loading into Ago, whereas the preferred 5′ nucleotide of the miRNA strand and the base‐pairing status in the seed region and the middle of the 3′ region function as additive anchors to Ago. Consequently, the miRNA authenticity is inspected at multiple steps during RISC assembly. MicroRNAs are loaded into the RISC complex in order to exert their gene‐silencing activity. The authors show that microRNA authenticity is checked at multiple steps during RISC assembly. MicroRNAs (miRNAs) function through the RNA‐induced silencing complex (RISC), which contains an Argonaute (Ago) protein at the core. RISC assembly follows a two‐step pathway: miRNA/miRNA * duplex loading into Ago, and separation of the two strands within Ago. Here we show that the 5′ phosphate of the miRNA strand is essential for duplex loading into Ago, whereas the preferred 5′ nucleotide of the miRNA strand and the base‐pairing status in the seed region and the middle of the 3′ region function as additive anchors to Ago. Consequently, the miRNA authenticity is inspected at multiple steps during RISC assembly. MicroRNAs are loaded into the RISC complex in order to exert their gene‐silencing activity. The authors show that microRNA authenticity is checked at multiple steps during RISC assembly. |
| Author | Yoda, Mayuko Kawamata, Tomoko Tomari, Yukihide |
| Author_xml | – sequence: 1 givenname: Tomoko surname: Kawamata fullname: Kawamata, Tomoko email: tomoko.kh@gmail.com organization: Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, 113-0032, Bunkyo-ku, Tokyo, Japan – sequence: 2 givenname: Mayuko surname: Yoda fullname: Yoda, Mayuko organization: Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, 113-0032, Bunkyo-ku, Tokyo, Japan – sequence: 3 givenname: Yukihide surname: Tomari fullname: Tomari, Yukihide email: tomoko.kh@gmail.com organization: Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, 113-0032, Bunkyo-ku, Tokyo, Japan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21738221$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1016/S0092-8674(03)00759-1 10.1016/j.molcel.2009.09.028 10.1016/S0092-8674(03)00801-8 10.1101/gad.1210204 10.1038/nature03462 10.1126/science.1102755 10.1016/j.cell.2007.05.057 10.1261/rna.1972910 10.1016/S0092-8674(01)00547-5 10.1016/S1046-2023(03)00052-5 10.1038/nature03514 10.1038/nature09039 10.1016/j.molcel.2010.05.014 10.1016/j.molcel.2010.05.015 10.1126/science.1102513 10.1016/j.molcel.2009.09.027 10.1016/j.molcel.2004.07.007 10.1016/j.tibs.2010.03.009 10.1038/nature07315 10.1038/nsmb.1630 10.1016/j.cell.2010.03.009 10.1016/j.cell.2009.01.002 10.1126/science.1065062 10.1038/nrm2632 10.1091/mbc.e09-10-0885 10.1038/nsmb.1733 |
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| References | Okamura K, Ishizuka A, Siomi H, Siomi MC (2004) Distinct roles for Argonaute proteins in small RNA-directed RNA cleavage pathways. Genes Dev 18: 1655-1666 Nykanen A, Haley B, Zamore PD (2001) ATP requirements and small interfering RNA structure in the RNA interference pathway. Cell 107: 309-321 Tomari Y, Du T, Zamore PD (2007) Sorting of Drosophila small silencing RNAs. Cell 130: 299-308 Iki T, Yoshikawa M, Nishikiori M, Jaudal MC, Matsumoto-Yokoyama E, Mitsuhara I, Meshi T, Ishikawa M (2010) In vitro assembly of plant RNA-induced silencing complexes facilitated by molecular chaperone HSP90. Mol Cell 39: 282-291 Ma JB, Yuan YR, Meister G, Pei Y, Tuschl T, Patel DJ (2005) Structural basis for 5′-end-specific recognition of guide RNA by the A. fulgidus Piwi protein. Nature 434: 666-670 Meister G, Landthaler M, Patkaniowska A, Dorsett Y, Teng G, Tuschl T (2004) Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs. Mol Cell 15: 185-197 Khvorova A, Reynolds A, Jayasena SD (2003) Functional siRNAs and miRNAs exhibit strand bias. Cell 115: 209-216 Ghildiyal M, Xu J, Seitz H, Weng Z, Zamore PD (2010) Sorting of Drosophila small silencing RNAs partitions microRNA* strands into the RNA interference pathway. RNA 16: 43-46 Hafner M et al (2010) Transcriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP. Cell 141: 129-141 Kawamata T, Seitz H, Tomari Y (2009) Structural determinants of miRNAs for RISC loading and slicer-independent unwinding. Nat Struct Mol Biol 16: 953-960 Haley B, Tang G, Zamore PD (2003) In vitro analysis of RNA interference in Drosophila melanogaster. Methods 30: 330-336 Kim VN, Han J, Siomi MC (2009) Biogenesis of small RNAs in animals. Nat Rev Mol Cell Biol 10: 126-139 Frank F, Sonenberg N, Nagar B (2010) Structural basis for 5′-nucleotide base-specific recognition of guide RNA by human AGO2. Nature 465: 818-822 Parker JS, Roe SM, Barford D (2005) Structural insights into mRNA recognition from a PIWI domain-siRNA guide complex. Nature 434: 663-666 Tomari Y, Matranga C, Haley B, Martinez N, Zamore PD (2004) A protein sensor for siRNA asymmetry. Science 306: 1377-1380 Liu J, Carmell MA, Rivas FV, Marsden CG, Thomson JM, Song JJ, Hammond SM, Joshua-Tor L, Hannon GJ (2004) Argonaute2 is the catalytic engine of mammalian RNAi. Science 305: 1437-1441 Czech B, Zhou R, Erlich Y, Brennecke J, Binari R, Villalta C, Gordon A, Perrimon N, Hannon GJ (2009) Hierarchical rules for Argonaute loading in Drosophila. Mol Cell 36: 445-456 Okamura K, Liu N, Lai EC (2009) Distinct mechanisms for microRNA strand selection by Drosophila Argonautes. Mol Cell 36: 431-444 Lau NC, Lim LP, Weinstein EG, Bartel DP (2001) An abundant class of tiny RNAs with probable regulatory roles in Caenorhabditis elegans. Science 294: 858-862 Johnston M, Geoffroy MC, Sobala A, Hay R, Hutvagner G (2010) HSP90 protein stabilizes unloaded Argonaute complexes and microscopic P-bodies in human cells. Mol Biol Cell 21: 1462-1469 Kawamata T, Tomari Y (2010) Making RISC. Trends Biochem Sci 35: 368-376 Wang Y, Sheng G, Juranek S, Tuschl T, Patel DJ (2008) Structure of the guide-strand-containing Argonaute silencing complex. Nature 456: 209-213 Yoda M, Kawamata T, Paroo Z, Ye X, Iwasaki S, Liu Q, Tomari Y (2010) ATP-dependent human RISC assembly pathways. Nat Struct Mol Biol 17: 17-23 Bartel DP (2009) MicroRNAs: target recognition and regulatory functions. Cell 136: 215-233 Iwasaki S, Kobayashi M, Yoda M, Sakaguchi Y, Katsuma S, Suzuki T, Tomari Y (2010) Hsc70/Hsp90 chaperone machinery mediates ATP-dependent RISC loading of small RNA duplexes. Mol Cell 39: 292-299 Schwarz DS, Hutvagner G, Du T, Xu Z, Aronin N, Zamore PD (2003) Asymmetry in the assembly of the RNAi enzyme complex. Cell 115: 199-208 Yoda, M, Kawamata, T, Paroo, Z, Ye, X, Iwasaki, S, Liu, Q, Tomari, Y (b26) 2010; 17 Khvorova, A, Reynolds, A, Jayasena, SD (b12) 2003; 115 Okamura, K, Liu, N, Lai, EC (b20) 2009; 36 Lau, NC, Lim, LP, Weinstein, EG, Bartel, DP (b14) 2001; 294 Frank, F, Sonenberg, N, Nagar, B (b3) 2010; 465 Meister, G, Landthaler, M, Patkaniowska, A, Dorsett, Y, Teng, G, Tuschl, T (b17) 2004; 15 Kawamata, T, Tomari, Y (b10) 2010; 35 Kawamata, T, Seitz, H, Tomari, Y (b11) 2009; 16 Johnston, M, Geoffroy, MC, Sobala, A, Hay, R, Hutvagner, G (b9) 2010; 21 Schwarz, DS, Hutvagner, G, Du, T, Xu, Z, Aronin, N, Zamore, PD (b22) 2003; 115 Iwasaki, S, Kobayashi, M, Yoda, M, Sakaguchi, Y, Katsuma, S, Suzuki, T, Tomari, Y (b8) 2010; 39 Tomari, Y, Du, T, Zamore, PD (b24) 2007; 130 Bartel, DP (b1) 2009; 136 Ma, JB, Yuan, YR, Meister, G, Pei, Y, Tuschl, T, Patel, DJ (b16) 2005; 434 Haley, B, Tang, G, Zamore, PD (b6) 2003; 30 Tomari, Y, Matranga, C, Haley, B, Martinez, N, Zamore, PD (b23) 2004; 306 Czech, B, Zhou, R, Erlich, Y, Brennecke, J, Binari, R, Villalta, C, Gordon, A, Perrimon, N, Hannon, GJ (b2) 2009; 36 Ghildiyal, M, Xu, J, Seitz, H, Weng, Z, Zamore, PD (b4) 2010; 16 Parker, JS, Roe, SM, Barford, D (b21) 2005; 434 Kim, VN, Han, J, Siomi, MC (b13) 2009; 10 Hafner, M (b5) 2010; 141 Liu, J, Carmell, MA, Rivas, FV, Marsden, CG, Thomson, JM, Song, JJ, Hammond, SM, Joshua-Tor, L, Hannon, GJ (b15) 2004; 305 Okamura, K, Ishizuka, A, Siomi, H, Siomi, MC (b19) 2004; 18 Nykanen, A, Haley, B, Zamore, PD (b18) 2001; 107 Wang, Y, Sheng, G, Juranek, S, Tuschl, T, Patel, DJ (b25) 2008; 456 Iki, T, Yoshikawa, M, Nishikiori, M, Jaudal, MC, Matsumoto-Yokoyama, E, Mitsuhara, I, Meshi, T, Ishikawa, M (b7) 2010; 39 2009; 36 2010; 21 2010; 16 2001; 294 2009; 10 2010; 35 2004; 18 2010; 39 2010; 17 2005; 434 2004; 15 2007; 130 2010; 465 2010; 141 2008; 456 2003; 115 2001; 107 2004; 306 2004; 305 2003; 30 2009; 136 2009; 16 15284456 - Science. 2004 Sep 3;305(5689):1437-41 20395147 - Trends Biochem Sci. 2010 Jul;35(7):368-76 15231716 - Genes Dev. 2004 Jul 15;18(14):1655-66 20237157 - Mol Biol Cell. 2010 May 1;21(9):1462-9 17662944 - Cell. 2007 Jul 27;130(2):299-308 15800628 - Nature. 2005 Mar 31;434(7033):663-6 14567918 - Cell. 2003 Oct 17;115(2):209-16 19917635 - RNA. 2010 Jan;16(1):43-56 11701122 - Cell. 2001 Nov 2;107(3):309-21 19684602 - Nat Struct Mol Biol. 2009 Sep;16(9):953-60 15550672 - Science. 2004 Nov 19;306(5700):1377-80 19917252 - Mol Cell. 2009 Nov 13;36(3):445-56 20605502 - Mol Cell. 2010 Jul 30;39(2):282-91 12828947 - Methods. 2003 Aug;30(4):330-6 20371350 - Cell. 2010 Apr 2;141(1):129-41 19167326 - Cell. 2009 Jan 23;136(2):215-33 15260970 - Mol Cell. 2004 Jul 23;15(2):185-97 19165215 - Nat Rev Mol Cell Biol. 2009 Feb;10(2):126-39 20605501 - Mol Cell. 2010 Jul 30;39(2):292-9 18754009 - Nature. 2008 Nov 13;456(7219):209-13 14567917 - Cell. 2003 Oct 17;115(2):199-208 19917251 - Mol Cell. 2009 Nov 13;36(3):431-44 20505670 - Nature. 2010 Jun 10;465(7299):818-22 11679671 - Science. 2001 Oct 26;294(5543):858-62 15800629 - Nature. 2005 Mar 31;434(7033):666-70 19966796 - Nat Struct Mol Biol. 2010 Jan;17(1):17-23 e_1_2_6_10_1 e_1_2_6_19_1 e_1_2_6_13_1 e_1_2_6_14_1 e_1_2_6_11_1 e_1_2_6_12_1 e_1_2_6_17_1 e_1_2_6_18_1 e_1_2_6_15_1 e_1_2_6_16_1 e_1_2_6_21_1 e_1_2_6_20_1 e_1_2_6_9_1 e_1_2_6_8_1 e_1_2_6_5_1 e_1_2_6_4_1 e_1_2_6_7_1 e_1_2_6_6_1 e_1_2_6_25_1 e_1_2_6_24_1 e_1_2_6_3_1 e_1_2_6_23_1 e_1_2_6_2_1 e_1_2_6_22_1 e_1_2_6_27_1 e_1_2_6_26_1 |
| References_xml | – volume: 16 start-page: 43 year: 2010 end-page: 46 ident: b4 publication-title: RNA contributor: fullname: Zamore, PD – volume: 16 start-page: 953 year: 2009 end-page: 960 ident: b11 publication-title: Nat Struct Mol Biol contributor: fullname: Tomari, Y – volume: 35 start-page: 368 year: 2010 end-page: 376 ident: b10 publication-title: Trends Biochem Sci contributor: fullname: Tomari, Y – volume: 36 start-page: 431 year: 2009 end-page: 444 ident: b20 publication-title: Mol Cell contributor: fullname: Lai, EC – volume: 434 start-page: 663 year: 2005 end-page: 666 ident: b21 publication-title: Nature contributor: fullname: Barford, D – volume: 107 start-page: 309 year: 2001 end-page: 321 ident: b18 publication-title: Cell contributor: fullname: Zamore, PD – volume: 39 start-page: 282 year: 2010 end-page: 291 ident: b7 publication-title: Mol Cell contributor: fullname: Ishikawa, M – volume: 21 start-page: 1462 year: 2010 end-page: 1469 ident: b9 publication-title: Mol Biol Cell contributor: fullname: Hutvagner, G – volume: 141 start-page: 129 year: 2010 end-page: 141 ident: b5 publication-title: Cell contributor: fullname: Hafner, M – volume: 465 start-page: 818 year: 2010 end-page: 822 ident: b3 publication-title: Nature contributor: fullname: Nagar, B – volume: 10 start-page: 126 year: 2009 end-page: 139 ident: b13 publication-title: Nat Rev Mol Cell Biol contributor: fullname: Siomi, MC – volume: 115 start-page: 199 year: 2003 end-page: 208 ident: b22 publication-title: Cell contributor: fullname: Zamore, PD – volume: 294 start-page: 858 year: 2001 end-page: 862 ident: b14 publication-title: Science contributor: fullname: Bartel, DP – volume: 136 start-page: 215 year: 2009 end-page: 233 ident: b1 publication-title: Cell contributor: fullname: Bartel, DP – volume: 434 start-page: 666 year: 2005 end-page: 670 ident: b16 publication-title: Nature contributor: fullname: Patel, DJ – volume: 305 start-page: 1437 year: 2004 end-page: 1441 ident: b15 publication-title: Science contributor: fullname: Hannon, GJ – volume: 15 start-page: 185 year: 2004 end-page: 197 ident: b17 publication-title: Mol Cell contributor: fullname: Tuschl, T – volume: 456 start-page: 209 year: 2008 end-page: 213 ident: b25 publication-title: Nature contributor: fullname: Patel, DJ – volume: 306 start-page: 1377 year: 2004 end-page: 1380 ident: b23 publication-title: Science contributor: fullname: Zamore, PD – volume: 18 start-page: 1655 year: 2004 end-page: 1666 ident: b19 publication-title: Genes Dev contributor: fullname: Siomi, MC – volume: 30 start-page: 330 year: 2003 end-page: 336 ident: b6 publication-title: Methods contributor: fullname: Zamore, PD – volume: 39 start-page: 292 year: 2010 end-page: 299 ident: b8 publication-title: Mol Cell contributor: fullname: Tomari, Y – volume: 130 start-page: 299 year: 2007 end-page: 308 ident: b24 publication-title: Cell contributor: fullname: Zamore, PD – volume: 36 start-page: 445 year: 2009 end-page: 456 ident: b2 publication-title: Mol Cell contributor: fullname: Hannon, GJ – volume: 115 start-page: 209 year: 2003 end-page: 216 ident: b12 publication-title: Cell contributor: fullname: Jayasena, SD – volume: 17 start-page: 17 year: 2010 end-page: 23 ident: b26 publication-title: Nat Struct Mol Biol contributor: fullname: Tomari, Y – volume: 36 start-page: 445 year: 2009 end-page: 456 article-title: Hierarchical rules for Argonaute loading in publication-title: Mol Cell – volume: 21 start-page: 1462 year: 2010 end-page: 1469 article-title: HSP90 protein stabilizes unloaded Argonaute complexes and microscopic P‐bodies in human cells publication-title: Mol Biol Cell – volume: 16 start-page: 953 year: 2009 end-page: 960 article-title: Structural determinants of miRNAs for RISC loading and slicer‐independent unwinding publication-title: Nat Struct Mol Biol – volume: 130 start-page: 299 year: 2007 end-page: 308 article-title: Sorting of small silencing RNAs publication-title: Cell – volume: 465 start-page: 818 year: 2010 end-page: 822 article-title: Structural basis for 5′‐nucleotide base‐specific recognition of guide RNA by human AGO2 publication-title: Nature – volume: 18 start-page: 1655 year: 2004 end-page: 1666 article-title: Distinct roles for Argonaute proteins in small RNA‐directed RNA cleavage pathways publication-title: Genes Dev – volume: 39 start-page: 292 year: 2010 end-page: 299 article-title: Hsc70/Hsp90 chaperone machinery mediates ATP‐dependent RISC loading of small RNA duplexes publication-title: Mol Cell – volume: 141 start-page: 129 year: 2010 end-page: 141 article-title: Transcriptome‐wide identification of RNA‐binding protein and microRNA target sites by PAR–CLIP publication-title: Cell – volume: 30 start-page: 330 year: 2003 end-page: 336 article-title: analysis of RNA interference in publication-title: Methods – volume: 10 start-page: 126 year: 2009 end-page: 139 article-title: Biogenesis of small RNAs in animals publication-title: Nat Rev Mol Cell Biol – volume: 15 start-page: 185 year: 2004 end-page: 197 article-title: Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs publication-title: Mol Cell – volume: 305 start-page: 1437 year: 2004 end-page: 1441 article-title: Argonaute2 is the catalytic engine of mammalian RNAi publication-title: Science – volume: 107 start-page: 309 year: 2001 end-page: 321 article-title: ATP requirements and small interfering RNA structure in the RNA interference pathway publication-title: Cell – volume: 39 start-page: 282 year: 2010 end-page: 291 article-title: assembly of plant RNA‐induced silencing complexes facilitated by molecular chaperone HSP90 publication-title: Mol Cell – volume: 115 start-page: 199 year: 2003 end-page: 208 article-title: Asymmetry in the assembly of the RNAi enzyme complex publication-title: Cell – volume: 17 start-page: 17 year: 2010 end-page: 23 article-title: ATP‐dependent human RISC assembly pathways publication-title: Nat Struct Mol Biol – volume: 456 start-page: 209 year: 2008 end-page: 213 article-title: Structure of the guide‐strand‐containing Argonaute silencing complex publication-title: Nature – volume: 136 start-page: 215 year: 2009 end-page: 233 article-title: MicroRNAs: target recognition and regulatory functions publication-title: Cell – volume: 16 start-page: 43 year: 2010 end-page: 46 article-title: Sorting of small silencing RNAs partitions microRNA strands into the RNA interference pathway publication-title: RNA – volume: 306 start-page: 1377 year: 2004 end-page: 1380 article-title: A protein sensor for siRNA asymmetry publication-title: Science – volume: 36 start-page: 431 year: 2009 end-page: 444 article-title: Distinct mechanisms for microRNA strand selection by Argonautes publication-title: Mol Cell – volume: 434 start-page: 666 year: 2005 end-page: 670 article-title: Structural basis for 5′‐end‐specific recognition of guide RNA by the Piwi protein publication-title: Nature – volume: 115 start-page: 209 year: 2003 end-page: 216 article-title: Functional siRNAs and miRNAs exhibit strand bias publication-title: Cell – volume: 434 start-page: 663 year: 2005 end-page: 666 article-title: Structural insights into mRNA recognition from a PIWI domain‐siRNA guide complex publication-title: Nature – volume: 35 start-page: 368 year: 2010 end-page: 376 article-title: Making RISC publication-title: Trends Biochem Sci – volume: 294 start-page: 858 year: 2001 end-page: 862 article-title: An abundant class of tiny RNAs with probable regulatory roles in publication-title: Science – ident: e_1_2_6_23_1 doi: 10.1016/S0092-8674(03)00759-1 – ident: e_1_2_6_3_1 doi: 10.1016/j.molcel.2009.09.028 – ident: e_1_2_6_13_1 doi: 10.1016/S0092-8674(03)00801-8 – ident: e_1_2_6_20_1 doi: 10.1101/gad.1210204 – ident: e_1_2_6_22_1 doi: 10.1038/nature03462 – ident: e_1_2_6_24_1 doi: 10.1126/science.1102755 – ident: e_1_2_6_25_1 doi: 10.1016/j.cell.2007.05.057 – ident: e_1_2_6_5_1 doi: 10.1261/rna.1972910 – ident: e_1_2_6_19_1 doi: 10.1016/S0092-8674(01)00547-5 – ident: e_1_2_6_7_1 doi: 10.1016/S1046-2023(03)00052-5 – ident: e_1_2_6_17_1 doi: 10.1038/nature03514 – ident: e_1_2_6_4_1 doi: 10.1038/nature09039 – ident: e_1_2_6_8_1 doi: 10.1016/j.molcel.2010.05.014 – ident: e_1_2_6_9_1 doi: 10.1016/j.molcel.2010.05.015 – ident: e_1_2_6_16_1 doi: 10.1126/science.1102513 – ident: e_1_2_6_21_1 doi: 10.1016/j.molcel.2009.09.027 – ident: e_1_2_6_18_1 doi: 10.1016/j.molcel.2004.07.007 – ident: e_1_2_6_11_1 doi: 10.1016/j.tibs.2010.03.009 – ident: e_1_2_6_26_1 doi: 10.1038/nature07315 – ident: e_1_2_6_12_1 doi: 10.1038/nsmb.1630 – ident: e_1_2_6_6_1 doi: 10.1016/j.cell.2010.03.009 – ident: e_1_2_6_2_1 doi: 10.1016/j.cell.2009.01.002 – ident: e_1_2_6_15_1 doi: 10.1126/science.1065062 – ident: e_1_2_6_14_1 doi: 10.1038/nrm2632 – ident: e_1_2_6_10_1 doi: 10.1091/mbc.e09-10-0885 – ident: e_1_2_6_27_1 doi: 10.1038/nsmb.1733 |
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| Snippet | MicroRNAs (miRNAs) function through the RNA‐induced silencing complex (RISC), which contains an Argonaute (Ago) protein at the core. RISC assembly follows a... MicroRNAs (miRNAs) function through the RNA-induced silencing complex (RISC), which contains an Argonaute (Ago) protein at the core. RISC assembly follows a... MicroRNAs are loaded into the RISC complex in order to exert their gene-silencing activity. The authors show that microRNA authenticity is checked at multiple... |
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| SubjectTerms | 5' Flanking Region Animals Argonaute Argonaute Proteins - metabolism Authenticity Base Pairing Drosophila melanogaster Embryo, Nonmammalian microRNA MicroRNAs - genetics MicroRNAs - metabolism Proteins Ribonucleic acid RISC RNA RNA, Messenger - metabolism RNA-Induced Silencing Complex - genetics RNA-Induced Silencing Complex - metabolism Scientific Reports |
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| Title | Multilayer checkpoints for microRNA authenticity during RISC assembly |
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