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Volumn 461, Issue 7265, 2009, Pages 823-827

Structural insights into mechanisms of the small RNA methyltransferase HEN1

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; LA ANTIGEN; MAGNESIUM ION; MICRORNA; PROTEIN HEN1; PROTEIN P19; RNA BINDING PROTEIN; RNA METHYLTRANSFERASE; S ADENOSYLHOMOCYSTEINE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 70349939426     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature08433     Document Type: Article
Times cited : (124)

References (38)
  • 1
    • 58449134534 scopus 로고    scopus 로고
    • Small silencing RNAs: An expanding universe
    • Ghildiyal, M. & Zamore, P. D. Small silencing RNAs: an expanding universe. Nature Rev. Genet. 10, 94-108 (2009).
    • (2009) Nature Rev. Genet. , vol.10 , pp. 94-108
    • Ghildiyal, M.1    Zamore, P.D.2
  • 2
    • 43049096410 scopus 로고    scopus 로고
    • The growing catalog of small RNAs and their association with distinct Argonaute/Piwi family members
    • Farazi, T. A., Juranek, S. A. & Tuschl, T. The growing catalog of small RNAs and their association with distinct Argonaute/Piwi family members. Development 135, 1201-1214 (2008).
    • (2008) Development , vol.135 , pp. 1201-1214
    • Farazi, T.A.1    Juranek, S.A.2    Tuschl, T.3
  • 3
    • 13644256193 scopus 로고    scopus 로고
    • Methylation as a crucial step in plant microRNA biogenesis
    • Yu, B. et al. Methylation as a crucial step in plant microRNA biogenesis. Science 307, 932-935 (2005).
    • (2005) Science , vol.307 , pp. 932-935
    • Yu, B.1
  • 4
    • 34447291602 scopus 로고    scopus 로고
    • The Drosophila RNA methyltransferase, DmHen1, modifies germline piRNAs and single-stranded siRNAs in RISC
    • Horwich, M. D. et al. The Drosophila RNA methyltransferase, DmHen1, modifies germline piRNAs and single-stranded siRNAs in RISC. Curr. Biol. 17, 1265-1272 (2007).
    • (2007) Curr. Biol. , vol.17 , pp. 1265-1272
    • Horwich, M.D.1
  • 5
    • 34347378274 scopus 로고    scopus 로고
    • Pimet, the Drosophila homolog of HEN1, mediates 2?-O-methylation of Piwi-interacting RNAs at their 39 ends
    • Saito, K. et al. Pimet, the Drosophila homolog of HEN1, mediates 2?-O-methylation of Piwi-interacting RNAs at their 39 ends. Genes Dev. 21, 1603-1608 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 1603-1608
    • Saito, K.1
  • 6
    • 34247259831 scopus 로고    scopus 로고
    • Mouse Piwi-interacting RNAs are 2?-O-methylated at their 39 termini
    • Kirino, Y. & Mourelatos, Z. Mouse Piwi-interacting RNAs are 2?-O-methylated at their 39 termini. Nature Struct. Mol. Biol. 14, 347-348 (2007).
    • (2007) Nature Struct. Mol. Biol. , vol.14 , pp. 347-348
    • Kirino, Y.1    Mourelatos, Z.2
  • 7
    • 34548366485 scopus 로고    scopus 로고
    • The mouse homolog of HEN1 is a potential methylase for Piwi-interacting RNAs
    • Kirino, Y. & Mourelatos, Z. The mouse homolog of HEN1 is a potential methylase for Piwi-interacting RNAs. RNA 13, 1397-1401 (2007).
    • (2007) RNA , vol.13 , pp. 1397-1401
    • Kirino, Y.1    Mourelatos, Z.2
  • 8
    • 62549159996 scopus 로고    scopus 로고
    • 2?-O-methylation stabilizes Piwi-associated small RNAs and ensures DNA elimination in Tetrahymena
    • Kurth, H. M. & Mochizuki, K. 2?-O-methylation stabilizes Piwi-associated small RNAs and ensures DNA elimination in Tetrahymena. RNA 15, 675-685 (2009).
    • (2009) RNA , vol.15 , pp. 675-685
    • Kurth, H.M.1    Mochizuki, K.2
  • 9
    • 0036339614 scopus 로고    scopus 로고
    • HEN1 functions pleiotropically in Arabidopsis development and acts in C function in the flower
    • Chen, X., Liu, J., Cheng, Y. & Jia, D. HEN1 functions pleiotropically in Arabidopsis development and acts in C function in the flower. Development 129, 1085-1094 (2002).
    • (2002) Development , vol.129 , pp. 1085-1094
    • Chen, X.1    Liu, J.2    Cheng, Y.3    Jia, D.4
  • 10
    • 0037015239 scopus 로고    scopus 로고
    • CARPEL FACTORY, a Dicer homolog, and HEN1, a novel protein, act in microRNA metabolism in Arabidopsis thaliana
    • Park, W., Li, J., Song, R., Messing, J. & Chen, X. CARPEL FACTORY, a Dicer homolog, and HEN1, a novel protein, act in microRNA metabolism in Arabidopsis thaliana. Curr. Biol. 12, 1484-1495 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 1484-1495
    • Park, W.1    Li, J.2    Song, R.3    Messing, J.4    Chen, X.5
  • 11
    • 32644454064 scopus 로고    scopus 로고
    • HEN1 recognizes 21-24 nt small RNA duplexes and deposits a methyl group onto the 2? OH of the 39 terminal nucleotide
    • Yang, Z., Ebright, Y. W., Yu, B. & Chen, X. HEN1 recognizes 21-24 nt small RNA duplexes and deposits a methyl group onto the 2? OH of the 39 terminal nucleotide. Nucleic Acids Res. 34, 667-675 (2006).
    • (2006) Nucleic Acids Res. , vol.34 , pp. 667-675
    • Yang, Z.1    Ebright, Y.W.2    Yu, B.3    Chen, X.4
  • 12
    • 23944493378 scopus 로고    scopus 로고
    • Methylation protects miRNAs and siRNAs from a 39-end uridylation activity in Arabidopsis
    • Li, J., Yang, Z., Yu, B., Liu, J. & Chen, X. Methylation protects miRNAs and siRNAs from a 39-end uridylation activity in Arabidopsis. Curr. Biol. 15, 1501-1507 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 1501-1507
    • Li, J.1    Yang, Z.2    Yu, B.3    Liu, J.4    Chen, X.5
  • 13
    • 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 321, 1490-1492 (2008).
    • (2008) Science , vol.321 , pp. 1490-1492
    • Ramachandran, V.1    Chen, X.2
  • 15
    • 33845755755 scopus 로고    scopus 로고
    • Molecular phylogenetics and comparative modeling of HEN1, a methyltransferase involved in plant microRNA biogenesis
    • Tkaczuk, K., Obarska, A. & Bujnicki, J. Molecular phylogenetics and comparative modeling of HEN1, a methyltransferase involved in plant microRNA biogenesis. BMC Evol. Biol. 6, 6 (2006).
    • (2006) BMC Evol. Biol. , vol.6 , pp. 6
    • Tkaczuk, K.1    Obarska, A.2    Bujnicki, J.3
  • 16
    • 57149093203 scopus 로고    scopus 로고
    • FKBP family proteins: Immunophilins with versatile biological functions
    • Kang, C. B., Dhe-Paganon, S. & Yoon, H. S. FKBP family proteins: immunophilins with versatile biological functions. Neurosignals 16, 318-325 (2008).
    • (2008) Neurosignals , vol.16 , pp. 318-325
    • Kang, C.B.1    Dhe-Paganon, S.2    Yoon, H.S.3
  • 18
    • 33745278074 scopus 로고    scopus 로고
    • A terminal affair: 39-end recognition by the human la protein
    • Curry, S. & Conte, M. R. A terminal affair: 39-end recognition by the human La protein. Trends Biochem. Sci. 31, 303-305 (2006).
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 303-305
    • Curry, S.1    Conte, M.R.2
  • 19
    • 30744449228 scopus 로고    scopus 로고
    • The la protein-RNA complex surfaces
    • Maraia, R. J. & Bayfield, M. A. The La protein-RNA complex surfaces. Mol. Cell 21, 149-152 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 149-152
    • Maraia, R.J.1    Bayfield, M.A.2
  • 20
    • 29544449398 scopus 로고    scopus 로고
    • Structural basis for recognition and sequestration of UUUOH 39 temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen
    • Teplova, M. et al. Structural basis for recognition and sequestration of UUUOH 39 temini of nascent RNA polymerase III transcripts by La, a rheumatic disease autoantigen. Mol. Cell 21, 75-85 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 75-85
    • Teplova, M.1
  • 21
    • 0347985826 scopus 로고    scopus 로고
    • Size selective recognition of siRNA by an RNA silencing suppressor
    • Vargason, J. M., Szittya, G., Burgyán, J. & Hall, T. M. T. Size selective recognition of siRNA by an RNA silencing suppressor. Cell 115, 799-811 (2003).
    • (2003) Cell , vol.115 , pp. 799-811
    • Vargason, J.M.1    Szittya, G.2    Burgyán, J.3    Hall, T.M.T.4
  • 22
    • 0347357615 scopus 로고    scopus 로고
    • Recognition of small interfering RNA by a viral suppressor of RNA silencing
    • Ye, K., Malinina, L. & Patel, D. J. Recognition of small interfering RNA by a viral suppressor of RNA silencing. Nature 426, 874-878 (2003).
    • (2003) Nature , vol.426 , pp. 874-878
    • Ye, K.1    Malinina, L.2    Patel, D.J.3
  • 23
    • 33646589610 scopus 로고    scopus 로고
    • Transgenically expressed viral RNA silencing suppressors interfere with microRNA methylation in Arabidopsis
    • Yu, B., Chapman, E. J., Yang, Z., Carrington, J. C. & Chen, X. Transgenically expressed viral RNA silencing suppressors interfere with microRNA methylation in Arabidopsis. FEBS Lett. 580, 3117-3120 (2006).
    • (2006) FEBS Lett. , vol.580 , pp. 3117-3120
    • Yu, B.1    Chapman, E.J.2    Yang, Z.3    Carrington, J.C.4    Chen, X.5
  • 24
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • Schubert, H. L., Blumenthal, R. M. & Cheng, X. Many paths to methyltransfer: a chronicle of convergence. Trends Biochem. Sci. 28, 329-335 (2003).
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 25
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA
    • Ryter, J. M. & Schultz, S. C. Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA. EMBO J. 17, 7505-7513 (1998).
    • (1998) EMBO J. , vol.17 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 26
    • 30844438338 scopus 로고    scopus 로고
    • Structural basis for double-stranded RNA processing by Dicer
    • MacRae, I. J. et al. Structural basis for double-stranded RNA processing by Dicer. Science 311, 195-198 (2006).
    • (2006) Science , vol.311 , pp. 195-198
    • MacRae, I.J.1
  • 28
    • 2442679207 scopus 로고    scopus 로고
    • Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain
    • Ma, J.-B., Ye, K. & Patel, D. J. Structural basis for overhang-specific small interfering RNA recognition by the PAZ domain. Nature 429, 318-322 (2004).
    • (2004) Nature , vol.429 , pp. 318-322
    • Ma, J.-B.1    Ye, K.2    Patel, D.J.3
  • 29
    • 42949086521 scopus 로고    scopus 로고
    • Approaches for studying microRNA and small interfering RNA methylation in vitro and in vivo
    • Yang, Z. et al. Approaches for studying microRNA and small interfering RNA methylation in vitro and in vivo. Methods Enzymol. 427, 139-154 (2007).
    • (2007) Methods Enzymol. , vol.427 , pp. 139-154
    • Yang, Z.1
  • 30
    • 12444276102 scopus 로고
    • Crosslinking of an iodo-uridine-RNA hairpin to a single site on the human U1A N-terminal RNA binding domain
    • Stump, W. T. & Hall, K. B. Crosslinking of an iodo-uridine-RNA hairpin to a single site on the human U1A N-terminal RNA binding domain. RNA 1, 55-63 (1995).
    • (1995) RNA , vol.1 , pp. 55-63
    • Stump, W.T.1    Hall, K.B.2
  • 31
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublié, S. & Carter, C. W. Jr. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276, 523-530 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1    Carter Jr., C.W.2
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., Minor, W. & Carter, C. W. Jr. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2    Carter Jr., C.W.3
  • 33
    • 0026095584 scopus 로고
    • Determination of macromolecular structures from anomalous diffraction of synthrotron radiation
    • Hendrickson, W. A. Determination of macromolecular structures from anomalous diffraction of synthrotron radiation. Science 254, 51-58 (1991).
    • (1991) Science , vol.254 , pp. 51-58
    • Hendrickson, W.A.1
  • 34
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams, P. D. et al. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr. D 58, 1948-1954 (2002).
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1948-1954
    • Adams, P.D.1
  • 35
    • 84889120137 scopus 로고
    • Improved methods for building protein models in eletron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in eletron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 36
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 37
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger, A. T. Version 1.2 of the Crystallography and NMR system. Nature Protocols 2, 2728-2733 (2007).
    • (2007) Nature Protocols , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 38
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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