메뉴 건너뛰기




Volumn 19, Issue 10, 2012, Pages 1011-1019

Dxo1 is a new type of eukaryotic enzyme with both decapping and 5′-3′ exoribonuclease activity

Author keywords

[No Author keywords available]

Indexed keywords

CELL ENZYME; INORGANIC PYROPHOSPHATASE; PROTEIN YDR370C; RNA; UNCLASSIFIED DRUG;

EID: 84867229926     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2381     Document Type: Article
Times cited : (78)

References (43)
  • 1
    • 0033788228 scopus 로고    scopus 로고
    • The ends of the affair: Capping and polyadenylation
    • Shatkin, A.J. & Manley, J.L. The ends of the affair: capping and polyadenylation. Nat. Struct. Biol. 7, 838-842 (2000).
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 838-842
    • Shatkin, A.J.1    Manley, J.L.2
  • 2
    • 0035787889 scopus 로고    scopus 로고
    • The mRNA capping apparatus as drug target and guide to eukaryotic phylogeny
    • Shuman, S. The mRNA capping apparatus as drug target and guide to eukaryotic phylogeny. Cold Spring Harb. Symp. Quant. Biol. 66, 301-312 (2001).
    • (2001) Cold Spring Harb. Symp. Quant. Biol. , vol.66 , pp. 301-312
    • Shuman, S.1
  • 4
    • 77958519530 scopus 로고    scopus 로고
    • Enzymology of RNA cap synthesis. Wiley Interdiscip
    • Ghosh, A. & Lima, C.D. Enzymology of RNA cap synthesis. Wiley Interdiscip. Rev. RNA 1, 152-172 (2010).
    • (2010) Rev. RNA , vol.1 , pp. 152-172
    • Ghosh, A.1    Lima, C.D.2
  • 5
  • 7
    • 56849103665 scopus 로고    scopus 로고
    • The control of mRNA decapping and P-body formation
    • Franks, T.M. & Lykke-Andersen, S. The control of mRNA decapping and P-body formation. Mol. Cell 32, 605-615 (2008).
    • (2008) Mol. Cell , vol.32 , pp. 605-615
    • Franks, T.M.1    Lykke-Andersen, S.2
  • 8
    • 60149090021 scopus 로고    scopus 로고
    • The many pathways of RNA degradation
    • Houseley, J. & Tollervey, D. The many pathways of RNA degradation. Cell 136, 763-776 (2009).
    • (2009) Cell , vol.136 , pp. 763-776
    • Houseley, J.1    Tollervey, D.2
  • 9
    • 84862832925 scopus 로고    scopus 로고
    • Regulation of mRNA decapping. Wiley Interdiscip
    • Li, Y. & Kiledjian, M. Regulation of mRNA decapping. Wiley Interdiscip. Rev. RNA 1, 253-265 (2010).
    • (2010) Rev. RNA , vol.1 , pp. 253-265
    • Li, Y.1    Kiledjian, M.2
  • 10
    • 0017842570 scopus 로고
    • An exoribonuclease from Saccharomyces cerevisiae: Effect of modifications of 5' end groups on the hydrolysis of substrates to 5' mononucleotides
    • Stevens, A. An exoribonuclease from Saccharomyces cerevisiae: effect of modifications of 5' end groups on the hydrolysis of substrates to 5' mononucleotides. Biochem. Biophys. Res. Commun. 81, 656-661 (1978).
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , pp. 656-661
    • Stevens, A.1
  • 11
    • 0018902741 scopus 로고
    • And characterization of a Saccharomyces cerevisiae exoribonuclease which yields 5'-mononucleotides by a 5'→3' mode of hydrolysis
    • Stevens, A. Purification and characterization of a Saccharomyces cerevisiae exoribonuclease which yields 5'-mononucleotides by a 5'→3' mode of hydrolysis. J. Biol. Chem. 255, 3080-3085 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 3080-3085
    • Stevens, A.1    Purification2
  • 12
    • 84866632974 scopus 로고    scopus 로고
    • 5'-3' exoribonucleases. in Ribonucleases
    • (ed. Nicholson, A.W.) Ch. 7 Springer
    • Chang, J.H., Xiang, S. & Tong, L. 5'-3' exoribonucleases. in Ribonucleases, Nucleic Acids and Molecular Biology Vol. 26 (ed. Nicholson, A.W.) Ch. 7, 167-192 (Springer, 2011).
    • (2011) Nucleic Acids and Molecular Biology , vol.26 , pp. 167-192
    • Chang, J.H.1    Xiang, S.2    Tong, L.3
  • 13
    • 78149426485 scopus 로고    scopus 로고
    • Multiple mRNA decapping enzymes in mammalian cells
    • Song, M.-G., Li, Y. & Kiledjian, M. Multiple mRNA decapping enzymes in mammalian cells. Mol. Cell 40, 423-432 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 423-432
    • Song, M.-G.1    Li, Y.2    Kiledjian, M.3
  • 14
    • 64749111945 scopus 로고    scopus 로고
    • Structure and function of the 5'→3' exoribonuclease Rat1 and its activating partner Rai1
    • Xiang, S. et al. Structure and function of the 5'→3' exoribonuclease Rat1 and its activating partner Rai1. Nature 458, 784-788 (2009).
    • (2009) Nature , vol.458 , pp. 784-788
    • Xiang, S.1
  • 15
    • 77957340903 scopus 로고    scopus 로고
    • Identification of a quality-control mechanism for mRNA 5'-end capping
    • Jiao, X. et al. Identification of a quality-control mechanism for mRNA 5'-end capping. Nature 467, 608-611 (2010).
    • (2010) Nature , vol.467 , pp. 608-611
    • Jiao, X.1
  • 16
    • 0034073993 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae RAI1 (YGL246c) is homologous to human DOM3Z and encodes a protein that binds the nuclear exoribonuclease Rat1p
    • Xue, Y. et al. Saccharomyces cerevisiae RAI1 (YGL246c) is homologous to human DOM3Z and encodes a protein that binds the nuclear exoribonuclease Rat1p. Mol. Cell. Biol. 20, 4006-4015 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4006-4015
    • Xue, Y.1
  • 17
    • 0142184341 scopus 로고    scopus 로고
    • Global analysis of protein localization in budding yeast
    • Huh, W.K. et al. Global analysis of protein localization in budding yeast. Nature 425, 686-691 (2003).
    • (2003) Nature , vol.425 , pp. 686-691
    • Huh, W.K.1
  • 18
    • 0034664813 scopus 로고    scopus 로고
    • Holliday junction resolvases and related nucleases: Identification of new families, phyletic distribution and evolutionary trajectories
    • Aravind, L., Makarova, K.S. & Koonin, E.V. Holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories. Nucleic Acids Res. 28, 3417-3432 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3417-3432
    • Aravind, L.1    Makarova, K.S.2    Koonin, E.V.3
  • 19
    • 68149163563 scopus 로고    scopus 로고
    • A bridge crosses the active-site canyon of the Epstein-Barr virus nuclease with DNase and RNase activities
    • Buisson, M. et al. A bridge crosses the active-site canyon of the Epstein-Barr virus nuclease with DNase and RNase activities. J. Mol. Biol. 391, 717-728 (2009).
    • (2009) J. Mol. Biol. , vol.391 , pp. 717-728
    • Buisson, M.1
  • 20
    • 70350435285 scopus 로고    scopus 로고
    • Crystal structure of the shutoff and exonuclease protein from the oncogenic Kaposi's sarcoma-associated herpesvirus
    • Dahlroth, S.-L., Gurmu, D., Haas, J., Erlandsen, H. & Nordlund, P. Crystal structure of the shutoff and exonuclease protein from the oncogenic Kaposi's sarcoma-associated herpesvirus. FEBS J. 276, 6636-6645 (2009).
    • (2009) FEBS J. , vol.276 , pp. 6636-6645
    • Dahlroth, S.-L.1    Gurmu, D.2    Haas, J.3    Erlandsen, H.4    Nordlund, P.5
  • 21
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • Holm, L., Kaariainen, S., Rosenstrom, P. & Schenkel, A. Searching protein structure databases with DaliLite v.3. Bioinformatics 24, 2780-2781 (2008).
    • (2008) Bioinformatics , vol.24 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 22
    • 65149086817 scopus 로고    scopus 로고
    • Crystal structure of E. coli RecE protein reveals a toroidal tetramer for processing double-stranded DNA breaks
    • Zhang, J., Xing, X., Herr, A.B. & Bell, C.E. Crystal structure of E. coli RecE protein reveals a toroidal tetramer for processing double-stranded DNA breaks. Structure 17, 690-702 (2009).
    • (2009) Structure , vol.17 , pp. 690-702
    • Zhang, J.1    Xing, X.2    Herr, A.B.3    Bell, C.E.4
  • 23
    • 0030881051 scopus 로고    scopus 로고
    • Toroidal structure of lambda-exonuclease
    • Kovall, R. & Matthews, B.W. Toroidal structure of lambda-exonuclease. Science 277, 1824-1827 (1997).
    • (1997) Science , vol.277 , pp. 1824-1827
    • Kovall, R.1    Matthews, B.W.2
  • 24
    • 0032848682 scopus 로고    scopus 로고
    • Type II restriction endonucleases: Structural, functional and evolutionary relationships
    • Kovall, R.A. & Matthews, B.W. Type II restriction endonucleases: structural, functional and evolutionary relationships. Curr. Opin. Chem. Biol. 3, 578-583 (1999).
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 578-583
    • Kovall, R.A.1    Matthews, B.W.2
  • 25
    • 33747689885 scopus 로고    scopus 로고
    • Alteration of sequence specificity of the type II restriction endonuclease HincII through an indirect readout mechanism
    • Joshi, H.K., Etzkorn, C., Chatwell, L., Bitinaite, J. & Horton, N.C. Alteration of sequence specificity of the type II restriction endonuclease HincII through an indirect readout mechanism. J. Biol. Chem. 281, 23852-23869 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 23852-23869
    • Joshi, H.K.1    Etzkorn, C.2    Chatwell, L.3    Bitinaite, J.4    Horton, N.C.5
  • 26
    • 70350090140 scopus 로고    scopus 로고
    • Real-time fluorescence detection of exoribonucleases
    • Sinturel, F. et al. Real-time fluorescence detection of exoribonucleases. RNA 15, 2057-2062 (2009).
    • (2009) RNA , vol.15 , pp. 2057-2062
    • Sinturel, F.1
  • 27
    • 79952362044 scopus 로고    scopus 로고
    • Structural and biochemical studies of the 5'→3' exoribonuclease Xrn1
    • Chang, J.H., Xiang, S., Xiang, K., Manley, J.L. & Tong, L. Structural and biochemical studies of the 5'→3' exoribonuclease Xrn1. Nat. Struct. Mol. Biol. 18, 270-276 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 270-276
    • Chang, J.H.1    Xiang, S.2    Xiang, K.3    Manley, J.L.4    Tong, L.5
  • 28
    • 19344365530 scopus 로고    scopus 로고
    • Connections between mRNA 3' end processing and transcription termination
    • Buratowski, S. Connections between mRNA 3' end processing and transcription termination. Curr. Opin. Cell Biol. 17, 257-261 (2005).
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 257-261
    • Buratowski, S.1
  • 29
    • 19344374029 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: Molecular insights and mechanistic variations across species
    • Conti, E. & Izaurralde, E. Nonsense-mediated mRNA decay: molecular insights and mechanistic variations across species. Curr. Opin. Cell Biol. 17, 316-325 (2005).
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 316-325
    • Conti, E.1    Izaurralde, E.2
  • 30
    • 34547623918 scopus 로고    scopus 로고
    • Quality control of eukaryotic mRNA: Safeguarding cells from abnormal mRNA function
    • Isken, O. & Maquat, L.E. Quality control of eukaryotic mRNA: safeguarding cells from abnormal mRNA function. Genes Dev. 21, 1833-1856 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 1833-1856
    • Isken, O.1    Maquat, L.E.2
  • 31
    • 79960065233 scopus 로고    scopus 로고
    • XUTs are a class of Xrn1-sensitive antisense regulatory non-coding RNA in yeast
    • van Dijk, E.L. et al. XUTs are a class of Xrn1-sensitive antisense regulatory non-coding RNA in yeast. Nature 475, 114-117 (2011).
    • (2011) Nature , vol.475 , pp. 114-117
    • Van Dijk, E.L.1
  • 32
    • 33845751052 scopus 로고    scopus 로고
    • Cytoplasmic decay of intergenic transcripts in Saccharomyces cerevisiae
    • Thompson, D.M. & Parker, R. Cytoplasmic decay of intergenic transcripts in Saccharomyces cerevisiae. Mol. Cell. Biol. 27, 92-101 (2007).
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 92-101
    • Thompson, D.M.1    Parker, R.2
  • 33
    • 0029916726 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9
    • Doublié, S. et al. Crystallization and preliminary X-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9. FEBS Lett. 384, 219-221 (1996).
    • (1996) FEBS Lett. , vol.384 , pp. 219-221
    • Doublié, S.1
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. 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
  • 35
    • 19944409045 scopus 로고    scopus 로고
    • The design and implementation of SnB v2.0
    • Weeks, C.M. & Miller, R. The design and implementation of SnB v2.0. J. Appl. Crystallogr. 32, 120-124 (1999).
    • (1999) J. Appl. Crystallogr. , vol.32 , pp. 120-124
    • Weeks, C.M.1    Miller, R.2
  • 36
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: Automated structure solution and density modification
    • Terwilliger, T.C. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374, 22-37 (2003).
    • (2003) Methods Enzymol. , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 37
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron 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 electron 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
  • 39
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR System: A new software suite for macromolecular structure determination
    • Brünger, A.T. et al. Crystallography & NMR System: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 40
    • 0033895727 scopus 로고    scopus 로고
    • Structure-function analysis of yeast mRNA cap methyltransferase and high-copy suppression of conditional mutants by AdoMet synthase and the ubiquitin conjugating enzyme Cdc34p
    • Schwer, B., Saha, N., Mao, X., Chen, H.W. & Shuman, S. Structure-function analysis of yeast mRNA cap methyltransferase and high-copy suppression of conditional mutants by AdoMet synthase and the ubiquitin conjugating enzyme Cdc34p. Genetics 155, 1561-1576 (2000).
    • (2000) Genetics , vol.155 , pp. 1561-1576
    • Schwer, B.1    Saha, N.2    Mao, X.3    Chen, H.W.4    Shuman, S.5
  • 41
    • 0026087180 scopus 로고
    • Preparation of high molecular weight RNA
    • Köhrer, K. & Domdey, H. Preparation of high molecular weight RNA. Methods Enzymol. 194, 398-405 (1991).
    • (1991) Methods Enzymol. , vol.194 , pp. 398-405
    • Köhrer, K.1    Domdey, H.2
  • 42
    • 0033066673 scopus 로고    scopus 로고
    • An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro
    • Wang, Z., Day, N., Trifillis, P. & Kiledjian, M. An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro. Mol. Cell. Biol. 19, 4552-4560 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4552-4560
    • Wang, Z.1    Day, N.2    Trifillis, P.3    Kiledjian, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.