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Volumn 42, Issue 5, 2014, Pages

A fluorescence-based assay suitable for quantitative analysis of deadenylase enzyme activity

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EID: 84892402977     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt972     Document Type: Article
Times cited : (28)

References (44)
  • 2
    • 41149138114 scopus 로고    scopus 로고
    • Multifunctional deadenylase complexes diversify mRNA control
    • Goldstrohm, A.C. and Wickens, M. (2008) Multifunctional deadenylase complexes diversify mRNA control. Nat. Rev. Mol Cell Biol., 9, 337-344.
    • (2008) Nat. Rev. Mol Cell Biol. , vol.9 , pp. 337-344
    • Goldstrohm, A.C.1    Wickens, M.2
  • 3
    • 0742288008 scopus 로고    scopus 로고
    • The enzymes and control of eukaryotic mRNA turnover
    • Parker, R. and Song, H. (2004) The enzymes and control of eukaryotic mRNA turnover. Nat. Struct. Mol. Biol., 11, 121-127.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 121-127
    • Parker, R.1    Song, H.2
  • 4
    • 84877801967 scopus 로고    scopus 로고
    • RNA decay machines: Deadenylation by the Ccr4-Not and Pan2-Pan3 complexes
    • Wahle, E. and Winkler, G.S. (2013) RNA decay machines: Deadenylation by the Ccr4-Not and Pan2-Pan3 complexes. Biochim. Biophys. Acta, 1829, 561-570.
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 561-570
    • Wahle, E.1    Winkler, G.S.2
  • 5
    • 84877806739 scopus 로고    scopus 로고
    • Kiss your tail goodbye: The role of PARN, Nocturnin, and Angel deadenylases in mRNA biology
    • Godwin, A.R., Kojima, S., Green, C.B. and Wilusz, J. (2013) Kiss your tail goodbye: The role of PARN, Nocturnin, and Angel deadenylases in mRNA biology. Biochim. Biophys. Acta, 1829, 571-579.
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 571-579
    • Godwin, A.R.1    Kojima, S.2    Green, C.B.3    Wilusz, J.4
  • 7
    • 0025310854 scopus 로고
    • MRNA poly(A) tail a 30 enhancer of translational initiation
    • Munroe, D. and Jacobson, A. (1990) mRNA poly(A) tail, a 30 enhancer of translational initiation. Mol. Cell Biol., 10, 3441-3455.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 3441-3455
    • Munroe, D.1    Jacobson, A.2
  • 8
    • 0037316406 scopus 로고    scopus 로고
    • Nocturnin a deadenylase in Xenopus laevis retina: A mechanism for posttranscriptional control of circadian-related mRNA
    • Baggs, J.E. and Green, C.B. (2003) Nocturnin, a deadenylase in Xenopus laevis retina: A mechanism for posttranscriptional control of circadian-related mRNA. Curr. Biol., 13, 189-198.
    • (2003) Curr. Biol. , vol.13 , pp. 189-198
    • Baggs, J.E.1    Green, C.B.2
  • 9
    • 80053219536 scopus 로고    scopus 로고
    • PDE12 removes mitochondrial RNA poly(A tails and controls translation in human mitochondria
    • Rorbach, J., Nicholls, T.J. and Minczuk, M. (2011) PDE12 removes mitochondrial RNA poly(A) tails and controls translation in human mitochondria. Nucleic Acids Res., 39, 7750-7763.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 7750-7763
    • Rorbach, J.1    Nicholls, T.J.2    Minczuk, M.3
  • 10
    • 84875618805 scopus 로고    scopus 로고
    • Poly(A)-specific ribonuclease (PARN): An allosterically regulated, processive and mRNA cap-interacting deadenylase
    • Virtanen, A., Henriksson, N., Nilsson, P. and Nissbeck, M. (2013) Poly(A)-specific ribonuclease (PARN): An allosterically regulated, processive and mRNA cap-interacting deadenylase. Crit. Rev. Biochem. Mol. Biol., 48, 192-209.
    • (2013) Crit. Rev. Biochem. Mol. Biol. , vol.48 , pp. 192-209
    • Virtanen, A.1    Henriksson, N.2    Nilsson, P.3    Nissbeck, M.4
  • 11
    • 0034161254 scopus 로고    scopus 로고
    • Cap-dependent deadenylation of mRNA
    • Dehlin, E., Wormington, M., Korner, C.G. and Wahle, E. (2000) Cap-dependent deadenylation of mRNA. EMBO J., 19, 1079-1086. (Pubitemid 30119832
    • (2000) EMBO Journal , vol.19 , Issue.5 , pp. 1079-1086
    • Dehlin, E.1    Wormington, M.2    Korner, C.G.3    Wahle, E.4
  • 12
    • 0035282971 scopus 로고    scopus 로고
    • A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements
    • DOI 10.1093/emboj/20.5.1134
    • Gao, M., Wilusz, C.J., Peltz, S.W. and Wilusz, J. (2001) A novel mRNA-decapping activity in HeLa cytoplasmic extracts is regulated by AU-rich elements. EMBO J., 20, 1134-1143. (Pubitemid 32186803
    • (2001) EMBO Journal , vol.20 , Issue.5 , pp. 1134-1143
    • Gao, M.1    Wilusz, C.J.2    Peltz, S.W.3    Wilusz, J.4
  • 13
    • 0035958843 scopus 로고    scopus 로고
    • The mRNA cap structure stimulates rate of poly(A removal and amplifies processivity of degradation
    • Martinez, J., Ren, Y.G., Nilsson, P., Ehrenberg, M. and Virtanen, A. (2001) The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation. J. Biol. Chem., 276, 27923-27929.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27923-27929
    • Martinez, J.1    Ren, Y.G.2    Nilsson, P.3    Ehrenberg, M.4    Virtanen, A.5
  • 14
    • 0029811599 scopus 로고    scopus 로고
    • PAN3 encodes a subunit of the Pab1p-dependent poly(A nuclease in Saccharomyces cerevisiae
    • Brown, C.E., Tarun, Jr. S.Z. Boeck, R. and Sachs, A.B. (1996) PAN3 encodes a subunit of the Pab1p-dependent poly(A) nuclease in Saccharomyces cerevisiae. Mol. Cell Biol., 16, 5744-5753.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 5744-5753
    • Brown, C.E.1    Tarun Jr., S.Z.2    Boeck, R.3    Sachs, A.B.4
  • 15
    • 0347093310 scopus 로고    scopus 로고
    • Identification of a human cytoplasmic poly(A nuclease complex stimulated by poly(A)-binding protein
    • Uchida, N., Hoshino, S. and Katada, T. (2004) Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein. J. Biol. Chem., 279, 1383-1391.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1383-1391
    • Uchida, N.1    Hoshino, S.2    Katada, T.3
  • 16
    • 0035830508 scopus 로고    scopus 로고
    • The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae
    • DOI 10.1016/S0092-8674(01)00225-2
    • Tucker, M., Valencia-Sanchez, M.A., Staples, R.R., Chen, J., Denis, C.L. and Parker, R. (2001) The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. Cell, 104, 377-386. (Pubitemid 32206458
    • (2001) Cell , vol.104 , Issue.3 , pp. 377-386
    • Tucker, M.1    Valencia-Sanchez, M.A.2    Staples, R.R.3    Chen, J.4    Denis, C.L.5    Parker, R.6
  • 18
    • 3543016170 scopus 로고    scopus 로고
    • A complex containing the CCR4 and CAF1 proteins is involved in mRNA deadenylation in Drosophila
    • DOI 10.1038/sj.emboj.7600273
    • Temme, C., Zaessinger, S., Meyer, S., Simonelig, M. and Wahle, E. (2004) A complex containing the CCR4 and CAF1 proteins is involved in mRNA deadenylation in Drosophila. EMBO J., 23, 2862-2871. (Pubitemid 39013558
    • (2004) EMBO Journal , vol.23 , Issue.14 , pp. 2862-2871
    • Temme, C.1    Zaessinger, S.2    Meyer, S.3    Simonelig, M.4    Wahle, E.5
  • 19
    • 77953629665 scopus 로고    scopus 로고
    • Subunits of the drosophila ccr4-not complex and their roles in mrna deadenylation
    • Temme, C., Zhang, L., Kremmer, E., Ihling, C., Chartier, A., Sinz, A., Simonelig, M. and Wahle, E. (2010) Subunits of the Drosophila CCR4-NOT complex and their roles in mRNA deadenylation. RNA, 16, 1356-1370.
    • (2010) RNA , vol.16 , pp. 1356-1370
    • Temme, C.1    Zhang, L.2    Kremmer, E.3    Ihling, C.4    Chartier, A.5    Sinz, A.6    Simonelig, M.7    Wahle, E.8
  • 20
    • 77955414308 scopus 로고    scopus 로고
    • The structural basis for deadenylation by the CCR4-NOT complex
    • Bartlam, M. and Yamamoto, T. (2010) The structural basis for deadenylation by the CCR4-NOT complex. Protein Cell, 1, 443-452.
    • (2010) Protein Cell , vol.1 , pp. 443-452
    • Bartlam, M.1    Yamamoto, T.2
  • 21
    • 84155195139 scopus 로고    scopus 로고
    • The Ccr4-not complex
    • Collart, M.A. and Panasenko, O.O. (2012) The Ccr4-not complex. Gene, 492, 42-53.
    • (2012) Gene , vol.492 , pp. 42-53
    • Collart, M.A.1    Panasenko, O.O.2
  • 23
    • 77955414733 scopus 로고    scopus 로고
    • Crystal structure of the human CNOT6L nuclease domain reveals strict poly(A substrate specificity
    • Wang, H., Morita, M., Yang, X., Suzuki, T., Yang, W., Wang, J., Ito, K., Wang, Q., Zhao, C., Bartlam, M. et al. (2010) Crystal structure of the human CNOT6L nuclease domain reveals strict poly(A) substrate specificity. EMBO J., 29, 2566-2576.
    • (2010) EMBO J. , vol.29 , pp. 2566-2576
    • Wang, H.1    Morita, M.2    Yang, X.3    Suzuki, T.4    Yang, W.5    Wang, J.6    Ito, K.7    Wang, Q.8    Zhao, C.9    Bartlam, M.10
  • 24
    • 84868094761 scopus 로고    scopus 로고
    • Architecture of the nuclease module of the yeast Ccr4-not complex: The Not1-Caf1-Ccr4 interaction
    • Basquin, J., Roudko, V.V., Rode, M., Basquin, C., Seraphin, B. and Conti, E. (2012) Architecture of the nuclease module of the yeast Ccr4-not complex: The Not1-Caf1-Ccr4 interaction. Mol. Cell, 48, 207-218.
    • (2012) Mol. Cell , vol.48 , pp. 207-218
    • Basquin, J.1    Roudko, V.V.2    Rode, M.3    Basquin, C.4    Seraphin, B.5    Conti, E.6
  • 25
    • 84870622730 scopus 로고    scopus 로고
    • The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex
    • Petit, A.P., Wohlbold, L., Bawankar, P., Huntzinger, E., Schmidt, S., Izaurralde, E. and Weichenrieder, O. (2012) The structural basis for the interaction between the CAF1 nuclease and the NOT1 scaffold of the human CCR4-NOT deadenylase complex. Nucleic Acids Res., 40, 11058-11072.
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11058-11072
    • Petit, A.P.1    Wohlbold, L.2    Bawankar, P.3    Huntzinger, E.4    Schmidt, S.5    Izaurralde, E.6    Weichenrieder, O.7
  • 27
    • 0029025449 scopus 로고
    • Identification of a mouse protein whose homolog in Saccharomyces cerevisiae is a component of the CCR4 transcriptional regulatory complex
    • Draper, M.P., Salvadore, C. and Denis, C.L. (1995) Identification of a mouse protein whose homolog in Saccharomyces cerevisiae is a component of the CCR4 transcriptional regulatory complex. Mol. Cell Biol., 15, 3487-3495.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 3487-3495
    • Draper, M.P.1    Salvadore, C.2    Denis, C.L.3
  • 28
    • 9144252209 scopus 로고    scopus 로고
    • Identification of four families of yCCR4-And Mg2+-dependent endonuclease-related proteins in higher eukaryotes, and characterization of orthologs of yCCR4 with a conserved leucine-rich repeat essential for hCAF1/hPOP2 binding
    • Dupressoir, A., Morel, A.P., Barbot, W., Loireau, M.P., Corbo, L. and Heidmann, T. (2001) Identification of four families of yCCR4-And Mg2+-dependent endonuclease-related proteins in higher eukaryotes, and characterization of orthologs of yCCR4 with a conserved leucine-rich repeat essential for hCAF1/hPOP2 binding. BMC Genomics, 2, 9.
    • (2001) BMC Genomics , vol.2 , pp. 9
    • Dupressoir, A.1    Morel, A.P.2    Barbot, W.3    Loireau, M.P.4    Corbo, L.5    Heidmann, T.6
  • 29
    • 70349337771 scopus 로고    scopus 로고
    • The ccr4-not deadenylase subunits cnot7 and cnot8 have overlapping roles and modulate cell proliferation
    • Aslam, A., Mittal, S., Koch, F., Andrau, J.C. and Winkler, G.S. (2009) The Ccr4-Not Deadenylase Subunits CNOT7 and CNOT8 Have Overlapping Roles and Modulate Cell Proliferation. Mol. Biol. Cell, 20, 3840-3850.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3840-3850
    • Aslam, A.1    Mittal, S.2    Koch, F.3    Andrau, J.C.4    Winkler, G.S.5
  • 30
    • 79952822512 scopus 로고    scopus 로고
    • The Ccr4a (CNOT6 and Ccr4b (CNOT6L) deadenylase subunits of the human Ccr4-Not complex contribute to the prevention of cell death and senescence
    • Mittal, S., Aslam, A., Doidge, R., Medica, R. and Winkler, G.S. (2011) The Ccr4a (CNOT6) and Ccr4b (CNOT6L) deadenylase subunits of the human Ccr4-Not complex contribute to the prevention of cell death and senescence. Mol. Biol. Cell, 22, 748-758.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 748-758
    • Mittal, S.1    Aslam, A.2    Doidge, R.3    Medica, R.4    Winkler, G.S.5
  • 31
    • 34347338699 scopus 로고    scopus 로고
    • Depletion of mammalian CCR4b deadenylase triggers elevation of the p27Kip1 mRNA level and impairs cell growth
    • Morita, M., Suzuki, T., Nakamura, T., Yokoyama, K., Miyasaka, T. and Yamamoto, T. (2007) Depletion of mammalian CCR4b deadenylase triggers elevation of the p27Kip1 mRNA level and impairs cell growth. Mol. Cell Biol., 27, 4980-4990.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 4980-4990
    • Morita, M.1    Suzuki, T.2    Nakamura, T.3    Yokoyama, K.4    Miyasaka, T.5    Yamamoto, T.6
  • 32
    • 33646435854 scopus 로고    scopus 로고
    • A nonradioactive assay for poly(a)-specific ribonuclease activity by methylene blue colorimetry
    • Cheng, Y., Liu, W.F., Yan, Y.B. and Zhou, H.M. (2006) A nonradioactive assay for poly(a)-specific ribonuclease activity by methylene blue colorimetry. Protein Pept. Lett., 13, 125-128.
    • (2006) Protein Pept. Lett. , vol.13 , pp. 125-128
    • Cheng, Y.1    Liu, W.F.2    Yan, Y.B.3    Zhou, H.M.4
  • 33
    • 0030586886 scopus 로고    scopus 로고
    • A general ribonuclease assay using methylene blue
    • Greiner-Stoeffele, T., Grunow, M. and Hahn, U. (1996) A general ribonuclease assay using methylene blue. Anal. Biochem., 240, 24-28.
    • (1996) Anal. Biochem. , vol.240 , pp. 24-28
    • Greiner-Stoeffele, T.1    Grunow, M.2    Hahn, U.3
  • 34
    • 84858600134 scopus 로고    scopus 로고
    • A deadenylase assay by sizeexclusion chromatography
    • He, G.J. and Yan, Y.B. (2012) A deadenylase assay by sizeexclusion chromatography. PLoS One, 7, e33700.
    • (2012) PLoS One , vol.7
    • He, G.J.1    Yan, Y.B.2
  • 35
    • 33745986334 scopus 로고    scopus 로고
    • Expression and purification of recombinant poly(A)-specific ribonuclease (PARN
    • Nilsson, P. and Virtanen, A. (2006) Expression and purification of recombinant poly(A)-specific ribonuclease (PARN) Int. J. Biol. Macromol., 39, 95-99.
    • (2006) Int. J. Biol. Macromol. , vol.39 , pp. 95-99
    • Nilsson, P.1    Virtanen, A.2
  • 36
    • 31544450787 scopus 로고    scopus 로고
    • Novel procedure for modeling ligand/receptor induced fit effects
    • Sherman, W., Day, T., Jacobson, M.P., Friesner, R.A. and Farid, R. (2006) Novel procedure for modeling ligand/receptor induced fit effects. J. Med. Chem., 49, 534-553.
    • (2006) J. Med. Chem. , vol.49 , pp. 534-553
    • Sherman, W.1    Day, T.2    Jacobson, M.P.3    Friesner, R.A.4    Farid, R.5
  • 38
    • 65249093782 scopus 로고    scopus 로고
    • The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn2+and Mn2+in the active site
    • Andersen, K.R., Jonstrup, A.T., Van, L.B. and Brodersen, D.E. (2009) The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn2+and Mn2+in the active site. RNA, 15, 850-861.
    • (2009) RNA , vol.15 , pp. 850-861
    • Andersen, K.R.1    Jonstrup, A.T.2    Van, L.B.3    Brodersen, D.E.4
  • 39
    • 34250670047 scopus 로고    scopus 로고
    • The 1.4-A crystal structure of the S pombe Pop2p deadenylase subunit unveils the configuration of an active enzyme
    • DOI 10.1093/nar/gkm178
    • Jonstrup, A.T., Andersen, K.R., Van, L.B. and Brodersen, D.E. (2007) The 1.4-A crystal structure of the S. pombe Pop2p deadenylase subunit unveils the configuration of an active enzyme. Nucleic Acids Res., 35, 3153-3164. (Pubitemid 47073652
    • (2007) Nucleic Acids Research , vol.35 , Issue.9 , pp. 3153-3164
    • Jonstrup, A.T.1    Andersen, K.R.2    Van, L.B.3    Brodersen, D.E.4
  • 40
    • 43449094029 scopus 로고    scopus 로고
    • Biophysical and biochemical characterization of recombinant human Pop2 deadenylase
    • Liu, W.F. and Yan, Y.B. (2008) Biophysical and biochemical characterization of recombinant human Pop2 deadenylase. Protein Expr. Purif., 60, 46-52.
    • (2008) Protein Expr. Purif. , vol.60 , pp. 46-52
    • Liu, W.F.1    Yan, Y.B.2
  • 41
    • 0025772751 scopus 로고
    • In vitro deadenylation of mammalian mRNA by a HeLa cell 30 exonuclease
    • Astrom, J., Astrom, A. and Virtanen, A. (1991) In vitro deadenylation of mammalian mRNA by a HeLa cell 30 exonuclease. EMBO J., 10, 3067-3071.
    • (1991) EMBO J. , vol.10 , pp. 3067-3071
    • Astrom, J.1    Astrom, A.2    Virtanen, A.3
  • 42
    • 0039535081 scopus 로고    scopus 로고
    • Poly(A tail shortening by a mammalian poly(A)-specific 30-exoribonuclease
    • Korner, C.G. and Wahle, E. (1997) Poly(A) tail shortening by a mammalian poly(A)-specific 30-exoribonuclease. J. Biol. Chem., 272, 10448-10456.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10448-10456
    • Korner, C.G.1    Wahle, E.2
  • 43
    • 83455172585 scopus 로고    scopus 로고
    • Kinetic and in silico analysis of the slow-binding inhibition of human poly(A)-specific ribonuclease (PARN by novel nucleoside analogues
    • Balatsos, N., Vlachakis, D., Chatzigeorgiou, V., Manta, S., Komiotis, D., Vlassi, M. and Stathopoulos, C. (2012) Kinetic and in silico analysis of the slow-binding inhibition of human poly(A)-specific ribonuclease (PARN) by novel nucleoside analogues. Biochimie, 94, 214-221.
    • (2012) Biochimie , vol.94 , pp. 214-221
    • Balatsos, N.1    Vlachakis, D.2    Chatzigeorgiou, V.3    Manta, S.4    Komiotis, D.5    Vlassi, M.6    Stathopoulos, C.7


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