메뉴 건너뛰기




Volumn 30, Issue 7, 2014, Pages 298-307

Eri1: A conserved enzyme at the crossroads of multiple RNA-processing pathways

Author keywords

Epigenetic regulation; Gene expression; Histone mRNA; MiRNA; RNAi; RRNA

Indexed keywords

3' 5' EXORIBONUCLEASE 1; EXORIBONUCLEASE; HISTONE; MICRORNA; RNA 5.8S; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; RIBOSOME RNA; RNA;

EID: 84903468502     PISSN: 01689525     EISSN: 13624555     Source Type: Journal    
DOI: 10.1016/j.tig.2014.05.003     Document Type: Review
Times cited : (29)

References (97)
  • 1
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: structural analysis and phylogenetic distribution
    • Zuo Y., Deutscher M.P. Exoribonuclease superfamilies: structural analysis and phylogenetic distribution. Nucleic Acids Res. 2001, 29:1017-1026.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2
  • 2
    • 0028862397 scopus 로고
    • The 3'-5' exonuclease site of DNA polymerase III from gram-positive bacteria: definition of a novel motif structure
    • Barnes M.H., et al. The 3'-5' exonuclease site of DNA polymerase III from gram-positive bacteria: definition of a novel motif structure. Gene 1995, 165:45-50.
    • (1995) Gene , vol.165 , pp. 45-50
    • Barnes, M.H.1
  • 3
    • 4644324017 scopus 로고    scopus 로고
    • Crystallographic structure of the nuclease domain of 3'hExo, a DEDDh family member, bound to rAMP
    • Cheng Y., Patel D.J. Crystallographic structure of the nuclease domain of 3'hExo, a DEDDh family member, bound to rAMP. J.Mol.Biol. 2004, 343:305-312.
    • (2004) J.Mol.Biol. , vol.343 , pp. 305-312
    • Cheng, Y.1    Patel, D.J.2
  • 4
    • 0141888419 scopus 로고    scopus 로고
    • A 3' exonuclease that specifically interacts with the 3' end of histone mRNA
    • Dominski Z., et al. A 3' exonuclease that specifically interacts with the 3' end of histone mRNA. Mol. Cell 2003, 12:295-305.
    • (2003) Mol. Cell , vol.12 , pp. 295-305
    • Dominski, Z.1
  • 5
    • 1342346710 scopus 로고    scopus 로고
    • A conserved siRNA-degrading RNase negatively regulates RNA interference in C. elegans
    • Kennedy S., et al. A conserved siRNA-degrading RNase negatively regulates RNA interference in C. elegans. Nature 2004, 427:645-649.
    • (2004) Nature , vol.427 , pp. 645-649
    • Kennedy, S.1
  • 6
    • 0033801353 scopus 로고    scopus 로고
    • SAF-Box, a conserved protein domain that specifically recognizes scaffold attachment region DNA
    • Kipp M., et al. SAF-Box, a conserved protein domain that specifically recognizes scaffold attachment region DNA. Mol. Cell. Biol. 2000, 20:7480-7489.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7480-7489
    • Kipp, M.1
  • 7
    • 0034161452 scopus 로고    scopus 로고
    • SAP: a putative DNA-binding motif involved in chromosomal organization
    • Aravind L., Koonin E.V. SAP: a putative DNA-binding motif involved in chromosomal organization. Trends Biochem. Sci. 2000, 25:112-114.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 112-114
    • Aravind, L.1    Koonin, E.V.2
  • 8
    • 33750044572 scopus 로고    scopus 로고
    • Characterization of 3'hExo, a 3' exonuclease specifically interacting with the 3' end of histone mRNA
    • Yang X.C., et al. Characterization of 3'hExo, a 3' exonuclease specifically interacting with the 3' end of histone mRNA. J. Biol. Chem. 2006, 281:30447-30454.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30447-30454
    • Yang, X.C.1
  • 9
    • 43249083987 scopus 로고    scopus 로고
    • Mouse Eri1 interacts with the ribosome and catalyzes 5.8S rRNA processing
    • Ansel K.M., et al. Mouse Eri1 interacts with the ribosome and catalyzes 5.8S rRNA processing. Nat. Struct. Mol. Biol. 2008, 15:523-530.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 523-530
    • Ansel, K.M.1
  • 10
    • 84872474666 scopus 로고    scopus 로고
    • Structure of histone mRNA stem-loop, human stem-loop binding protein, and 3'hExo ternary complex
    • Tan D., et al. Structure of histone mRNA stem-loop, human stem-loop binding protein, and 3'hExo ternary complex. Science 2013, 339:318-321.
    • (2013) Science , vol.339 , pp. 318-321
    • Tan, D.1
  • 11
    • 0027751663 scopus 로고
    • The C. elegans heterochronic gene lin-4 encodes small RNAs with antisense complementarity to lin-14
    • Lee R.C., et al. The C. elegans heterochronic gene lin-4 encodes small RNAs with antisense complementarity to lin-14. Cell 1993, 75:843-854.
    • (1993) Cell , vol.75 , pp. 843-854
    • Lee, R.C.1
  • 12
    • 0032545933 scopus 로고    scopus 로고
    • Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    • Fire A., et al. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature 1998, 391:806-811.
    • (1998) Nature , vol.391 , pp. 806-811
    • Fire, A.1
  • 13
    • 0027730383 scopus 로고
    • Posttranscriptional regulation of the heterochronic gene lin-14 by lin-4 mediates temporal pattern formation in C. elegans
    • Wightman B., et al. Posttranscriptional regulation of the heterochronic gene lin-14 by lin-4 mediates temporal pattern formation in C. elegans. Cell 1993, 75:855-862.
    • (1993) Cell , vol.75 , pp. 855-862
    • Wightman, B.1
  • 14
    • 84880723481 scopus 로고    scopus 로고
    • Biology and Mechanisms of Short RNAs in Caenorhabditis elegans
    • Grishok A. Biology and Mechanisms of Short RNAs in Caenorhabditis elegans. Adv. Genet. 2013, 83:1-69.
    • (2013) Adv. Genet. , vol.83 , pp. 1-69
    • Grishok, A.1
  • 15
    • 44349159416 scopus 로고    scopus 로고
    • Pseudogene-derived small interfering RNAs regulate gene expression in mouse oocytes
    • Tam O.H., et al. Pseudogene-derived small interfering RNAs regulate gene expression in mouse oocytes. Nature 2008, 453:534-538.
    • (2008) Nature , vol.453 , pp. 534-538
    • Tam, O.H.1
  • 16
    • 44349130233 scopus 로고    scopus 로고
    • Endogenous siRNAs from naturally formed dsRNAs regulate transcripts in mouse oocytes
    • Watanabe T., et al. Endogenous siRNAs from naturally formed dsRNAs regulate transcripts in mouse oocytes. Nature 2008, 453:539-543.
    • (2008) Nature , vol.453 , pp. 539-543
    • Watanabe, T.1
  • 17
    • 31044452870 scopus 로고    scopus 로고
    • Functional proteomics reveals the biochemical niche of C. elegans DCR-1 in multiple small-RNA-mediated pathways
    • Duchaine T.F., et al. Functional proteomics reveals the biochemical niche of C. elegans DCR-1 in multiple small-RNA-mediated pathways. Cell 2006, 124:343-354.
    • (2006) Cell , vol.124 , pp. 343-354
    • Duchaine, T.F.1
  • 18
    • 33645464445 scopus 로고    scopus 로고
    • Interacting endogenous and exogenous RNAi pathways in Caenorhabditis elegans
    • Lee R.C., et al. Interacting endogenous and exogenous RNAi pathways in Caenorhabditis elegans. RNA 2006, 12:589-597.
    • (2006) RNA , vol.12 , pp. 589-597
    • Lee, R.C.1
  • 19
    • 0037031152 scopus 로고    scopus 로고
    • Loss of the putative RNA-directed RNA polymerase RRF-3 makes C. elegans hypersensitive to RNAi
    • Simmer F., et al. Loss of the putative RNA-directed RNA polymerase RRF-3 makes C. elegans hypersensitive to RNAi. Curr. Biol. 2002, 12:1317-1319.
    • (2002) Curr. Biol. , vol.12 , pp. 1317-1319
    • Simmer, F.1
  • 20
    • 73249136094 scopus 로고    scopus 로고
    • 26G endo-siRNAs regulate spermatogenic and zygotic gene expression in Caenorhabditis elegans
    • Han T., et al. 26G endo-siRNAs regulate spermatogenic and zygotic gene expression in Caenorhabditis elegans. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:18674-18679.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 18674-18679
    • Han, T.1
  • 21
    • 70349476898 scopus 로고    scopus 로고
    • Distinct argonaute-mediated 22G-RNA pathways direct genome surveillance in the C. elegans germline
    • Gu W., et al. Distinct argonaute-mediated 22G-RNA pathways direct genome surveillance in the C. elegans germline. Mol. Cell 2009, 36:231-244.
    • (2009) Mol. Cell , vol.36 , pp. 231-244
    • Gu, W.1
  • 22
    • 84855432200 scopus 로고    scopus 로고
    • Tudor domain ERI-5 tethers an RNA-dependent RNA polymerase to DCR-1 to potentiate endo-RNAi
    • Thivierge C., et al. Tudor domain ERI-5 tethers an RNA-dependent RNA polymerase to DCR-1 to potentiate endo-RNAi. Nat. Struct. Mol. Biol. 2012, 19:90-97.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 90-97
    • Thivierge, C.1
  • 23
    • 71549147194 scopus 로고    scopus 로고
    • Requirement for the ERI/DICER complex in endogenous RNA interference and sperm development in Caenorhabditis elegans
    • Pavelec D.M., et al. Requirement for the ERI/DICER complex in endogenous RNA interference and sperm development in Caenorhabditis elegans. Genetics 2009, 183:1283-1295.
    • (2009) Genetics , vol.183 , pp. 1283-1295
    • Pavelec, D.M.1
  • 24
    • 20844434177 scopus 로고    scopus 로고
    • Transcriptional silencing of nonsense codon-containing immunoglobulin minigenes
    • Bühler M., et al. Transcriptional silencing of nonsense codon-containing immunoglobulin minigenes. Mol. Cell 2005, 18:307-317.
    • (2005) Mol. Cell , vol.18 , pp. 307-317
    • Bühler, M.1
  • 25
    • 25844450312 scopus 로고    scopus 로고
    • High doses of siRNAs induce eri-1 and adar-1 gene expression and reduce the efficiency of RNA interference in the mouse
    • Hong J., et al. High doses of siRNAs induce eri-1 and adar-1 gene expression and reduce the efficiency of RNA interference in the mouse. Biochem. J. 2005, 390:675-679.
    • (2005) Biochem. J. , vol.390 , pp. 675-679
    • Hong, J.1
  • 26
    • 43249092177 scopus 로고    scopus 로고
    • The exonuclease ERI-1 has a conserved dual role in 5.8S rRNA processing and RNAi
    • Gabel H.W., Ruvkun G. The exonuclease ERI-1 has a conserved dual role in 5.8S rRNA processing and RNAi. Nat. Struct. Mol. Biol. 2008, 15:531-533.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 531-533
    • Gabel, H.W.1    Ruvkun, G.2
  • 27
    • 77649253620 scopus 로고    scopus 로고
    • Distinct phases of siRNA synthesis in an endogenous RNAi pathway in C. elegans soma
    • Gent J.I., et al. Distinct phases of siRNA synthesis in an endogenous RNAi pathway in C. elegans soma. Mol. Cell 2010, 37:679-689.
    • (2010) Mol. Cell , vol.37 , pp. 679-689
    • Gent, J.I.1
  • 28
    • 84863594456 scopus 로고    scopus 로고
    • Eri1 regulates microRNA homeostasis and mouse lymphocyte development and anti-viral function
    • Thomas M.F., et al. Eri1 regulates microRNA homeostasis and mouse lymphocyte development and anti-viral function. Blood 2012, 120:130-142.
    • (2012) Blood , vol.120 , pp. 130-142
    • Thomas, M.F.1
  • 29
    • 34250877841 scopus 로고    scopus 로고
    • A mammalian microRNA expression atlas based on small RNA library sequencing
    • Landgraf P., et al. A mammalian microRNA expression atlas based on small RNA library sequencing. Cell 2007, 129:1401-1414.
    • (2007) Cell , vol.129 , pp. 1401-1414
    • Landgraf, P.1
  • 30
    • 51749093103 scopus 로고    scopus 로고
    • Degradation of microRNAs by a family of exoribonucleases in Arabidopsis
    • Ramachandran V., Chen X. Degradation of microRNAs by a family of exoribonucleases in Arabidopsis. Science 2008, 321:1490-1492.
    • (2008) Science , vol.321 , pp. 1490-1492
    • Ramachandran, V.1    Chen, X.2
  • 31
    • 70349453924 scopus 로고    scopus 로고
    • Active turnover modulates mature microRNA activity in Caenorhabditis elegans
    • Chatterjee S., Grosshans H. Active turnover modulates mature microRNA activity in Caenorhabditis elegans. Nature 2009, 461:546-549.
    • (2009) Nature , vol.461 , pp. 546-549
    • Chatterjee, S.1    Grosshans, H.2
  • 32
    • 0347361541 scopus 로고    scopus 로고
    • Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs
    • Yi R., et al. Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs. Genes Dev. 2003, 17:3011-3016.
    • (2003) Genes Dev. , vol.17 , pp. 3011-3016
    • Yi, R.1
  • 33
    • 70849093653 scopus 로고    scopus 로고
    • A high-resolution structure of the pre-microRNA nuclear export machinery
    • Okada C., et al. A high-resolution structure of the pre-microRNA nuclear export machinery. Science 2009, 326:1275-1279.
    • (2009) Science , vol.326 , pp. 1275-1279
    • Okada, C.1
  • 34
    • 0345359925 scopus 로고    scopus 로고
    • Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain
    • Lingel A., et al. Structure and nucleic-acid binding of the Drosophila Argonaute 2 PAZ domain. Nature 2003, 426:465-469.
    • (2003) Nature , vol.426 , pp. 465-469
    • Lingel, A.1
  • 35
    • 0345490960 scopus 로고    scopus 로고
    • The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexes
    • Song J.J., et al. The crystal structure of the Argonaute2 PAZ domain reveals an RNA binding motif in RNAi effector complexes. Nat. Struct. Biol. 2003, 10:1026-1032.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 1026-1032
    • Song, J.J.1
  • 36
    • 2442679207 scopus 로고    scopus 로고
    • Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain
    • Ma J.B., et al. Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain. Nature 2004, 429:318-322.
    • (2004) Nature , vol.429 , pp. 318-322
    • Ma, J.B.1
  • 37
    • 70349820140 scopus 로고    scopus 로고
    • Lin28 recruits the TUTase Zcchc11 to inhibit let-7 maturation in mouse embryonic stem cells
    • Hagan J.P., et al. Lin28 recruits the TUTase Zcchc11 to inhibit let-7 maturation in mouse embryonic stem cells. Nat. Struct. Mol. Biol. 2009, 16:1021-1025.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1021-1025
    • Hagan, J.P.1
  • 38
    • 68749102148 scopus 로고    scopus 로고
    • TUT4 in concert with Lin28 suppresses microRNA biogenesis through pre-microRNA uridylation
    • Heo I., et al. TUT4 in concert with Lin28 suppresses microRNA biogenesis through pre-microRNA uridylation. Cell 2009, 138:696-708.
    • (2009) Cell , vol.138 , pp. 696-708
    • Heo, I.1
  • 39
    • 69949154245 scopus 로고    scopus 로고
    • Zcchc11-dependent uridylation of microRNA directs cytokine expression
    • Jones M.R., et al. Zcchc11-dependent uridylation of microRNA directs cytokine expression. Nat. Cell Biol. 2009, 11:1157-1163.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1157-1163
    • Jones, M.R.1
  • 40
    • 70349810911 scopus 로고    scopus 로고
    • LIN-28 and the poly(U) polymerase PUP-2 regulate let-7 microRNA processing in Caenorhabditis elegans
    • Lehrbach N.J., et al. LIN-28 and the poly(U) polymerase PUP-2 regulate let-7 microRNA processing in Caenorhabditis elegans. Nat. Struct. Mol. Biol. 2009, 16:1016-1020.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1016-1020
    • Lehrbach, N.J.1
  • 41
    • 78650446573 scopus 로고    scopus 로고
    • The human cytoplasmic RNA terminal U-transferase ZCCHC11 targets histone mRNAs for degradation
    • Schmidt M.J., et al. The human cytoplasmic RNA terminal U-transferase ZCCHC11 targets histone mRNAs for degradation. RNA 2011, 17:39-44.
    • (2011) RNA , vol.17 , pp. 39-44
    • Schmidt, M.J.1
  • 42
    • 84859865972 scopus 로고    scopus 로고
    • RNAi in fission yeast finds new targets and new ways of targeting at the nuclear periphery
    • Holoch D., Moazed D. RNAi in fission yeast finds new targets and new ways of targeting at the nuclear periphery. Genes Dev. 2012, 26:741-745.
    • (2012) Genes Dev. , vol.26 , pp. 741-745
    • Holoch, D.1    Moazed, D.2
  • 43
    • 58749097426 scopus 로고    scopus 로고
    • Small RNAs in transcriptional gene silencing and genome defence
    • Moazed D. Small RNAs in transcriptional gene silencing and genome defence. Nature 2009, 457:413-420.
    • (2009) Nature , vol.457 , pp. 413-420
    • Moazed, D.1
  • 44
    • 84860353476 scopus 로고    scopus 로고
    • Different means, same end-heterochromatin formation by RNAi and RNAi-independent RNA processing factors in fission yeast
    • Reyes-Turcu F.E., Grewal S.I. Different means, same end-heterochromatin formation by RNAi and RNAi-independent RNA processing factors in fission yeast. Curr. Opin. Genet. Dev. 2012, 22:156-163.
    • (2012) Curr. Opin. Genet. Dev. , vol.22 , pp. 156-163
    • Reyes-Turcu, F.E.1    Grewal, S.I.2
  • 45
    • 33746016283 scopus 로고    scopus 로고
    • Conserved ribonuclease, Eri1, negatively regulates heterochromatin assembly in fission yeast
    • Iida T., et al. Conserved ribonuclease, Eri1, negatively regulates heterochromatin assembly in fission yeast. Curr. Biol. 2006, 16:1459-1464.
    • (2006) Curr. Biol. , vol.16 , pp. 1459-1464
    • Iida, T.1
  • 46
    • 33646923128 scopus 로고    scopus 로고
    • Tethering RITS to a nascent transcript initiates RNAi- and heterochromatin-dependent gene silencing
    • Bühler M., et al. Tethering RITS to a nascent transcript initiates RNAi- and heterochromatin-dependent gene silencing. Cell 2006, 125:873-886.
    • (2006) Cell , vol.125 , pp. 873-886
    • Bühler, M.1
  • 47
    • 80054791942 scopus 로고    scopus 로고
    • High-dose siRNAs upregulate mouse Eri-1 at both transcription and posttranscription levels
    • Bian Y., et al. High-dose siRNAs upregulate mouse Eri-1 at both transcription and posttranscription levels. PLoS ONE 2011, 6:e26466.
    • (2011) PLoS ONE , vol.6
    • Bian, Y.1
  • 48
    • 0036719183 scopus 로고    scopus 로고
    • Ngl2p is a Ccr4p-like RNA nuclease essential for the final step in 3'-end processing of 5.8S rRNA in Saccharomyces cerevisiae
    • Faber A.W., et al. Ngl2p is a Ccr4p-like RNA nuclease essential for the final step in 3'-end processing of 5.8S rRNA in Saccharomyces cerevisiae. RNA 2002, 8:1095-1101.
    • (2002) RNA , vol.8 , pp. 1095-1101
    • Faber, A.W.1
  • 49
    • 79955537355 scopus 로고    scopus 로고
    • Ribosome-mediated specificity in Hox mRNA translation and vertebrate tissue patterning
    • Kondrashov N., et al. Ribosome-mediated specificity in Hox mRNA translation and vertebrate tissue patterning. Cell 2011, 145:383-397.
    • (2011) Cell , vol.145 , pp. 383-397
    • Kondrashov, N.1
  • 50
    • 24644480213 scopus 로고    scopus 로고
    • Inhibition of translational initiation by Let-7 MicroRNA in human cells
    • Pillai R.S., et al. Inhibition of translational initiation by Let-7 MicroRNA in human cells. Science 2005, 309:1573-1576.
    • (2005) Science , vol.309 , pp. 1573-1576
    • Pillai, R.S.1
  • 51
    • 0023666061 scopus 로고
    • Histone H2B repression causes cell-cycle-specific arrest in yeast: effects on chromosomal segregation, replication, and transcription
    • Han M., et al. Histone H2B repression causes cell-cycle-specific arrest in yeast: effects on chromosomal segregation, replication, and transcription. Cell 1987, 48:589-597.
    • (1987) Cell , vol.48 , pp. 589-597
    • Han, M.1
  • 52
    • 19344366158 scopus 로고    scopus 로고
    • Metazoan replication-dependent histone mRNAs: a distinct set of RNA polymerase II transcripts
    • Marzluff W.F. Metazoan replication-dependent histone mRNAs: a distinct set of RNA polymerase II transcripts. Curr. Opin. Cell Biol. 2005, 17:274-280.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 274-280
    • Marzluff, W.F.1
  • 53
    • 0023579211 scopus 로고
    • Identification of the human U7 snRNP as one of several factors involved in the 3' end maturation of histone premessenger RNA's
    • Mowry K.L., Steitz J.A. Identification of the human U7 snRNP as one of several factors involved in the 3' end maturation of histone premessenger RNA's. Science 1987, 238:1682-1687.
    • (1987) Science , vol.238 , pp. 1682-1687
    • Mowry, K.L.1    Steitz, J.A.2
  • 54
    • 0034128749 scopus 로고    scopus 로고
    • Stem-loop binding protein, the protein that binds the 3' end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms
    • Whitfield M.L., et al. Stem-loop binding protein, the protein that binds the 3' end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms. Mol. Cell. Biol. 2000, 20:4188-4198.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4188-4198
    • Whitfield, M.L.1
  • 55
    • 0023236379 scopus 로고
    • Properties of the exonuclease activity that degrades H4 histone mRNA
    • Ross J., et al. Properties of the exonuclease activity that degrades H4 histone mRNA. J. Biol. Chem. 1987, 262:9374-9381.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9374-9381
    • Ross, J.1
  • 56
    • 0023666085 scopus 로고
    • Translation is required for regulation of histone mRNA degradation
    • Graves R.A., et al. Translation is required for regulation of histone mRNA degradation. Cell 1987, 48:615-626.
    • (1987) Cell , vol.48 , pp. 615-626
    • Graves, R.A.1
  • 57
    • 23344452109 scopus 로고    scopus 로고
    • Translation termination is involved in histone mRNA degradation when DNA replication is inhibited
    • Kaygun H., Marzluff W.F. Translation termination is involved in histone mRNA degradation when DNA replication is inhibited. Mol. Cell. Biol. 2005, 25:6879-6888.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6879-6888
    • Kaygun, H.1    Marzluff, W.F.2
  • 58
    • 84872026333 scopus 로고    scopus 로고
    • Eri1 degrades the stem-loop of oligouridylated histone mRNAs to induce replication-dependent decay
    • Hoefig K.P., et al. Eri1 degrades the stem-loop of oligouridylated histone mRNAs to induce replication-dependent decay. Nat. Struct. Mol. Biol. 2013, 20:73-81.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 73-81
    • Hoefig, K.P.1
  • 59
    • 38149023239 scopus 로고    scopus 로고
    • Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'
    • Mullen T.E., Marzluff W.F. Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'. Genes Dev. 2008, 22:50-65.
    • (2008) Genes Dev. , vol.22 , pp. 50-65
    • Mullen, T.E.1    Marzluff, W.F.2
  • 60
    • 77949538979 scopus 로고    scopus 로고
    • Engineered rings of mixed yeast Lsm proteins show differential interactions with translation factors and U-rich RNA
    • Sobti M., et al. Engineered rings of mixed yeast Lsm proteins show differential interactions with translation factors and U-rich RNA. Biochemistry 2010, 49:2335-2345.
    • (2010) Biochemistry , vol.49 , pp. 2335-2345
    • Sobti, M.1
  • 61
    • 84888412297 scopus 로고    scopus 로고
    • 3'-End processing of histone pre-mRNAs in Drosophila: U7 snRNP is associated with FLASH and polyadenylation factors
    • Sabath I., et al. 3'-End processing of histone pre-mRNAs in Drosophila: U7 snRNP is associated with FLASH and polyadenylation factors. RNA 2013, 19:1726-1744.
    • (2013) RNA , vol.19 , pp. 1726-1744
    • Sabath, I.1
  • 62
    • 58449134534 scopus 로고    scopus 로고
    • Small silencing RNAs: an expanding universe
    • Ghildiyal M., Zamore P.D. Small silencing RNAs: an expanding universe. Nat. Rev. Genet. 2009, 10:94-108.
    • (2009) Nat. Rev. Genet. , vol.10 , pp. 94-108
    • Ghildiyal, M.1    Zamore, P.D.2
  • 63
    • 70350510820 scopus 로고    scopus 로고
    • RNAi in budding yeast
    • Drinnenberg I., et al. RNAi in budding yeast. Science 2009, 326:544-550.
    • (2009) Science , vol.326 , pp. 544-550
    • Drinnenberg, I.1
  • 64
    • 80052956817 scopus 로고    scopus 로고
    • Compatibility with killer explains the rise of RNAi-deficient fungi
    • Drinnenberg I.A., et al. Compatibility with killer explains the rise of RNAi-deficient fungi. Science 2011, 333:1592.
    • (2011) Science , vol.333 , pp. 1592
    • Drinnenberg, I.A.1
  • 65
    • 23944506289 scopus 로고    scopus 로고
    • RNA interference is an antiviral defence mechanism in Caenorhabditis elegans
    • Wilkins C., et al. RNA interference is an antiviral defence mechanism in Caenorhabditis elegans. Nature 2005, 436:1044-1047.
    • (2005) Nature , vol.436 , pp. 1044-1047
    • Wilkins, C.1
  • 66
    • 0344688414 scopus 로고    scopus 로고
    • A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae
    • Gunjan A., Verreault A. A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae. Cell 2003, 115:537-549.
    • (2003) Cell , vol.115 , pp. 537-549
    • Gunjan, A.1    Verreault, A.2
  • 67
    • 33845264383 scopus 로고    scopus 로고
    • Genetic and biochemical characterization of Drosophila Snipper: a promiscuous member of the metazoan 3'hExo/ERI-1 family of 3' to 5' exonucleases
    • Kupsco J.M., et al. Genetic and biochemical characterization of Drosophila Snipper: a promiscuous member of the metazoan 3'hExo/ERI-1 family of 3' to 5' exonucleases. RNA 2006, 12:2103-2117.
    • (2006) RNA , vol.12 , pp. 2103-2117
    • Kupsco, J.M.1
  • 68
    • 0018797508 scopus 로고
    • Sequence and secondary structure of Drosophila melanogaster 5.8S and 2S rRNAs and of the processing site between them
    • Pavlakis G.N., et al. Sequence and secondary structure of Drosophila melanogaster 5.8S and 2S rRNAs and of the processing site between them. Nucleic Acids Res. 1979, 7:2213-2238.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 2213-2238
    • Pavlakis, G.N.1
  • 69
    • 84860323000 scopus 로고    scopus 로고
    • Reduced expression of ribosomal proteins relieves microRNA-mediated repression
    • Janas M.M., et al. Reduced expression of ribosomal proteins relieves microRNA-mediated repression. Mol. Cell 2012, 46:171-186.
    • (2012) Mol. Cell , vol.46 , pp. 171-186
    • Janas, M.M.1
  • 70
    • 0034711308 scopus 로고    scopus 로고
    • Human RNase III is a 160-kDa protein involved in preribosomal RNA processing
    • Wu H., et al. Human RNase III is a 160-kDa protein involved in preribosomal RNA processing. J. Biol. Chem. 2000, 275:36957-36965.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36957-36965
    • Wu, H.1
  • 71
    • 34247876168 scopus 로고    scopus 로고
    • DEAD-box RNA helicase subunits of the Drosha complex are required for processing of rRNA and a subset of microRNAs
    • Fukuda T., et al. DEAD-box RNA helicase subunits of the Drosha complex are required for processing of rRNA and a subset of microRNAs. Nat. Cell Biol. 2007, 9:604-611.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 604-611
    • Fukuda, T.1
  • 72
    • 84864688599 scopus 로고    scopus 로고
    • DGCR8 HITS-CLIP reveals novel functions for the Microprocessor
    • Macias S., et al. DGCR8 HITS-CLIP reveals novel functions for the Microprocessor. Nat Struct Mol Biol 2012, 19:760-766.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 760-766
    • Macias, S.1
  • 73
    • 79959455595 scopus 로고    scopus 로고
    • Depletion of key protein components of the RISC pathway impairs pre-ribosomal RNA processing
    • Liang X.H., Crooke S.T. Depletion of key protein components of the RISC pathway impairs pre-ribosomal RNA processing. Nucleic Acids Res. 2011, 39:4875-4889.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 4875-4889
    • Liang, X.H.1    Crooke, S.T.2
  • 74
    • 84856005348 scopus 로고    scopus 로고
    • Candida albicans Dicer (CaDcr1) is required for efficient ribosomal and spliceosomal RNA maturation
    • Bernstein D.A., et al. Candida albicans Dicer (CaDcr1) is required for efficient ribosomal and spliceosomal RNA maturation. Proc. Natl. Acad. Sci. U.S.A. 2011, 109:523-528.
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 523-528
    • Bernstein, D.A.1
  • 75
    • 0032557455 scopus 로고    scopus 로고
    • Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8S rRNA 3' end formation
    • Briggs M.W., et al. Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8S rRNA 3' end formation. J. Biol. Chem. 1998, 273:13255-13263.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13255-13263
    • Briggs, M.W.1
  • 76
    • 77955500933 scopus 로고    scopus 로고
    • MicroRNA biogenesis via splicing and exosome-mediated trimming in Drosophila
    • Flynt A.S., et al. MicroRNA biogenesis via splicing and exosome-mediated trimming in Drosophila. Mol. Cell 2010, 38:900-907.
    • (2010) Mol. Cell , vol.38 , pp. 900-907
    • Flynt, A.S.1
  • 77
    • 73649109602 scopus 로고    scopus 로고
    • A mammalian herpesvirus uses noncanonical expression and processing mechanisms to generate viral MicroRNAs
    • Bogerd H.P., et al. A mammalian herpesvirus uses noncanonical expression and processing mechanisms to generate viral MicroRNAs. Mol. Cell 2010, 37:135-142.
    • (2010) Mol. Cell , vol.37 , pp. 135-142
    • Bogerd, H.P.1
  • 78
    • 58149097010 scopus 로고    scopus 로고
    • Posttranscriptional crossregulation between Drosha and DGCR8
    • Han J., et al. Posttranscriptional crossregulation between Drosha and DGCR8. Cell 2009, 136:75-84.
    • (2009) Cell , vol.136 , pp. 75-84
    • Han, J.1
  • 79
    • 62549120015 scopus 로고    scopus 로고
    • Genome-wide identification of targets of the drosha-pasha/DGCR8 complex
    • Kadener S., et al. Genome-wide identification of targets of the drosha-pasha/DGCR8 complex. RNA 2009, 15:537-545.
    • (2009) RNA , vol.15 , pp. 537-545
    • Kadener, S.1
  • 80
    • 66449118741 scopus 로고    scopus 로고
    • Post-transcriptional control of DGCR8 expression by the Microprocessor
    • Triboulet R., et al. Post-transcriptional control of DGCR8 expression by the Microprocessor. RNA 2009, 15:1005-1011.
    • (2009) RNA , vol.15 , pp. 1005-1011
    • Triboulet, R.1
  • 81
    • 84855877366 scopus 로고    scopus 로고
    • Ars2 promotes proper replication-dependent histone mRNA 3' end formation
    • Gruber J.J., et al. Ars2 promotes proper replication-dependent histone mRNA 3' end formation. Mol. Cell 2012, 45:87-98.
    • (2012) Mol. Cell , vol.45 , pp. 87-98
    • Gruber, J.J.1
  • 82
    • 67650638926 scopus 로고    scopus 로고
    • Ars2 regulates both miRNA- and siRNA-dependent silencing and suppresses RNA virus infection in Drosophila
    • Sabin L.R., et al. Ars2 regulates both miRNA- and siRNA-dependent silencing and suppresses RNA virus infection in Drosophila. Cell 2009, 138:340-351.
    • (2009) Cell , vol.138 , pp. 340-351
    • Sabin, L.R.1
  • 83
    • 67650590937 scopus 로고    scopus 로고
    • Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation
    • Gruber J.J., et al. Ars2 links the nuclear cap-binding complex to RNA interference and cell proliferation. Cell 2009, 138:328-339.
    • (2009) Cell , vol.138 , pp. 328-339
    • Gruber, J.J.1
  • 84
    • 34249025702 scopus 로고    scopus 로고
    • Contribution of Trf4/5 and the nuclear exosome to genome stability through regulation of histone mRNA levels in Saccharomyces cerevisiae
    • Reis C.C., Campbell J.L. Contribution of Trf4/5 and the nuclear exosome to genome stability through regulation of histone mRNA levels in Saccharomyces cerevisiae. Genetics 2007, 175:993-1010.
    • (2007) Genetics , vol.175 , pp. 993-1010
    • Reis, C.C.1    Campbell, J.L.2
  • 85
    • 35548957338 scopus 로고    scopus 로고
    • Deletion of the nuclear exosome component RRP6 leads to continued accumulation of the histone mRNA HTB1 in S-phase of the cell cycle in Saccharomyces cerevisiae
    • Canavan R., Bond U. Deletion of the nuclear exosome component RRP6 leads to continued accumulation of the histone mRNA HTB1 in S-phase of the cell cycle in Saccharomyces cerevisiae. Nucleic Acids Res. 2007, 35:6268-6279.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 6268-6279
    • Canavan, R.1    Bond, U.2
  • 86
    • 48249126187 scopus 로고    scopus 로고
    • The RNA-binding proteins HYL1 and SE promote accurate in vitro processing of pri-miRNA by DCL1
    • Dong Z., et al. The RNA-binding proteins HYL1 and SE promote accurate in vitro processing of pri-miRNA by DCL1. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:9970-9975.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9970-9975
    • Dong, Z.1
  • 87
    • 80053210329 scopus 로고    scopus 로고
    • Molecular insights into miRNA processing by Arabidopsis thaliana SERRATE
    • Machida S., et al. Molecular insights into miRNA processing by Arabidopsis thaliana SERRATE. Nucleic Acids Res. 2011, 39:7828-7836.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 7828-7836
    • Machida, S.1
  • 88
    • 67650642156 scopus 로고    scopus 로고
    • Ars2 and the Cap-binding complex team up for silencing
    • Nielsen A.F., et al. Ars2 and the Cap-binding complex team up for silencing. Cell 2009, 138:224-226.
    • (2009) Cell , vol.138 , pp. 224-226
    • Nielsen, A.F.1
  • 89
    • 53949088050 scopus 로고    scopus 로고
    • Lin28 mediates the terminal uridylation of let-7 precursor MicroRNA
    • Heo I., et al. Lin28 mediates the terminal uridylation of let-7 precursor MicroRNA. Mol. Cell 2008, 32:276-284.
    • (2008) Mol. Cell , vol.32 , pp. 276-284
    • Heo, I.1
  • 90
    • 84877757514 scopus 로고    scopus 로고
    • A role for the Perlman syndrome exonuclease Dis3l2 in the Lin28-let-7 pathway
    • Chang H.M., et al. A role for the Perlman syndrome exonuclease Dis3l2 in the Lin28-let-7 pathway. Nature 2013, 497:244-248.
    • (2013) Nature , vol.497 , pp. 244-248
    • Chang, H.M.1
  • 91
    • 84880245419 scopus 로고    scopus 로고
    • The exoribonuclease Dis3L2 defines a novel eukaryotic RNA degradation pathway
    • Malecki M., et al. The exoribonuclease Dis3L2 defines a novel eukaryotic RNA degradation pathway. EMBO J. 2013, 32:1842-1854.
    • (2013) EMBO J. , vol.32 , pp. 1842-1854
    • Malecki, M.1
  • 92
    • 84880224541 scopus 로고    scopus 로고
    • Exonuclease hDIS3L2 specifies an exosome-independent 3'-5' degradation pathway of human cytoplasmic mRNA
    • Lubas M., et al. Exonuclease hDIS3L2 specifies an exosome-independent 3'-5' degradation pathway of human cytoplasmic mRNA. EMBO J. 2013, 32:1855-1868.
    • (2013) EMBO J. , vol.32 , pp. 1855-1868
    • Lubas, M.1
  • 93
    • 84887608523 scopus 로고    scopus 로고
    • Poly(A)-specific ribonuclease mediates 3'-end trimming of Argonaute2-cleaved precursor microRNAs
    • Yoda M., et al. Poly(A)-specific ribonuclease mediates 3'-end trimming of Argonaute2-cleaved precursor microRNAs. Cell Rep. 2013, 5:715-726.
    • (2013) Cell Rep. , vol.5 , pp. 715-726
    • Yoda, M.1
  • 94
    • 84886301873 scopus 로고    scopus 로고
    • Argonaute and Triman generate dicer-independent priRNAs and mature siRNAs to initiate heterochromatin formation
    • Marasovic M., et al. Argonaute and Triman generate dicer-independent priRNAs and mature siRNAs to initiate heterochromatin formation. Mol. Cell 2013, 52:173-183.
    • (2013) Mol. Cell , vol.52 , pp. 173-183
    • Marasovic, M.1
  • 95
    • 66849122924 scopus 로고    scopus 로고
    • Decapping is preceded by 3' uridylation in a novel pathway of bulk mRNA turnover
    • Rissland O.S., Norbury C.J. Decapping is preceded by 3' uridylation in a novel pathway of bulk mRNA turnover. Nat. Struct. Mol. Biol. 2009, 16:616-623.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 616-623
    • Rissland, O.S.1    Norbury, C.J.2
  • 96
    • 0024253664 scopus 로고
    • Uridylation of U6 RNA in a nuclear extract in Ehrlich ascites tumor cells
    • Hirai H., et al. Uridylation of U6 RNA in a nuclear extract in Ehrlich ascites tumor cells. J. Biochem. 1988, 104:991-994.
    • (1988) J. Biochem. , vol.104 , pp. 991-994
    • Hirai, H.1
  • 97
    • 84857379318 scopus 로고    scopus 로고
    • Widespread RNA 3'-end oligouridylation in mammals
    • Choi Y.S., et al. Widespread RNA 3'-end oligouridylation in mammals. RNA 2012, 18:394-401.
    • (2012) RNA , vol.18 , pp. 394-401
    • Choi, Y.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.