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Volumn 2, Issue 1, 2011, Pages 106-123

Exonucleases and endonucleases involved in polyadenylation- assisted RNA decay

Author keywords

[No Author keywords available]

Indexed keywords

ENDONUCLEASE; EXONUCLEASE; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; RIBONUCLEASE; RIBONUCLEASE III;

EID: 81255198360     PISSN: 17577004     EISSN: 17577012     Source Type: Journal    
DOI: 10.1002/wrna.45     Document Type: Review
Times cited : (14)

References (136)
  • 1
    • 0037184518 scopus 로고    scopus 로고
    • The poly(A) tail of mRNAs: bodyguard in eukaryotes, scavenger in bacteria
    • Dreyfus M, Regnier P. The poly(A) tail of mRNAs: bodyguard in eukaryotes, scavenger in bacteria. Cell 2002, 111:611-613.
    • (2002) Cell , vol.111 , pp. 611-613
    • Dreyfus, M.1    Regnier, P.2
  • 2
    • 15244343863 scopus 로고    scopus 로고
    • mRNA decay in prokaryotes and eukaryotes: different approaches to a similar problem
    • Kushner SR. mRNA decay in prokaryotes and eukaryotes: different approaches to a similar problem. IUBMB Life 2004, 56:585-594.
    • (2004) IUBMB Life , vol.56 , pp. 585-594
    • Kushner, S.R.1
  • 3
    • 30344450374 scopus 로고    scopus 로고
    • RNA polyadenylation in prokaryotes and organelles; different tails tell different tales
    • Slomovic S, Portnoy V, Liveanu V, Schuster G. RNA polyadenylation in prokaryotes and organelles; different tails tell different tales. CRC Crit Rev Plant Sci 2006, 25:65-77.
    • (2006) CRC Crit Rev Plant Sci , vol.25 , pp. 65-77
    • Slomovic, S.1    Portnoy, V.2    Liveanu, V.3    Schuster, G.4
  • 4
    • 0033551137 scopus 로고    scopus 로고
    • Oligoribonuclease is an essential component of the mRNA decay pathway
    • Ghosh S, Deutscher MP. Oligoribonuclease is an essential component of the mRNA decay pathway. Proc Natl Acad Sci U S A 1999, 96:4372-4377.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 4372-4377
    • Ghosh, S.1    Deutscher, M.P.2
  • 5
    • 0036364652 scopus 로고    scopus 로고
    • A history of poly A sequences: from formation to factors to function
    • Edmonds M. A history of poly A sequences: from formation to factors to function. Prog Nucleic Acid Res Mol Biol 2002, 71:285-389.
    • (2002) Prog Nucleic Acid Res Mol Biol , vol.71 , pp. 285-389
    • Edmonds, M.1
  • 6
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 2009, 136:731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 7
    • 22544448652 scopus 로고    scopus 로고
    • Polyadenylation and degradation of human mitochondrial RNA: the prokaryotic past leaves its mark
    • Slomovic S, Laufer D, Geiger D, Schuster G. Polyadenylation and degradation of human mitochondrial RNA: the prokaryotic past leaves its mark. Mol Cell Biol 2005, 25:6427-6435.
    • (2005) Mol Cell Biol , vol.25 , pp. 6427-6435
    • Slomovic, S.1    Laufer, D.2    Geiger, D.3    Schuster, G.4
  • 9
    • 60149090021 scopus 로고    scopus 로고
    • The many pathways of RNA degradation
    • Houseley J, Tollervey D. The many pathways of RNA degradation. Cell 2009, 136:763-776.
    • (2009) Cell , vol.136 , pp. 763-776
    • Houseley, J.1    Tollervey, D.2
  • 10
    • 54149091257 scopus 로고    scopus 로고
    • Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail
    • Marzluff WF, Wagner EJ, Duronio RJ. Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail. Nat Rev Genet 2008, 9:843-854.
    • (2008) Nat Rev Genet , vol.9 , pp. 843-854
    • Marzluff, W.F.1    Wagner, E.J.2    Duronio, R.J.3
  • 11
    • 38149137954 scopus 로고    scopus 로고
    • New ways to meet your (3′) end oligouridylation as a step on the path to destruction
    • Wilusz CJ, Wilusz J. New ways to meet your (3′) end oligouridylation as a step on the path to destruction. Genes Dev 2008, 22:1-7.
    • (2008) Genes Dev , vol.22 , pp. 1-7
    • Wilusz, C.J.1    Wilusz, J.2
  • 12
    • 75949116417 scopus 로고    scopus 로고
    • Polyadenylation and degradation of incomplete RNA polymerase I transcripts in mammalian cells
    • Shcherbik N, Wang M, Lapik YR, Srivastava L, Pestov DG. Polyadenylation and degradation of incomplete RNA polymerase I transcripts in mammalian cells. EMBO Rep 2010, 11:106-111.
    • (2010) EMBO Rep , vol.11 , pp. 106-111
    • Shcherbik, N.1    Wang, M.2    Lapik, Y.R.3    Srivastava, L.4    Pestov, D.G.5
  • 14
    • 33749535437 scopus 로고    scopus 로고
    • CUT it out: silencing of noise in the transcriptome
    • Lykke-Andersen S, Jensen TH. CUT it out: silencing of noise in the transcriptome. Nat Struct Mol Biol 2006, 13:860-861.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 860-861
    • Lykke-Andersen, S.1    Jensen, T.H.2
  • 16
    • 33748424364 scopus 로고    scopus 로고
    • Termination of cryptic unstable transcripts is directed by yeast RNA-binding proteins Nrd1 and Nab3
    • Arigo JT, Eyler DE, Carroll KL, Corden JL. Termination of cryptic unstable transcripts is directed by yeast RNA-binding proteins Nrd1 and Nab3. Mol Cell 2006, 23:841-851.
    • (2006) Mol Cell , vol.23 , pp. 841-851
    • Arigo, J.T.1    Eyler, D.E.2    Carroll, K.L.3    Corden, J.L.4
  • 17
    • 33748435751 scopus 로고    scopus 로고
    • Transcription termination and nuclear degradation of cryptic unstable transcripts: a role for the nrd1-nab3 pathway in genome surveillance
    • Thiebaut M, Kisseleva-Romanova E, Rougemaille M, Boulay J, Libri D. Transcription termination and nuclear degradation of cryptic unstable transcripts: a role for the nrd1-nab3 pathway in genome surveillance. Mol Cell 2006, 23:853-864.
    • (2006) Mol Cell , vol.23 , pp. 853-864
    • Thiebaut, M.1    Kisseleva-Romanova, E.2    Rougemaille, M.3    Boulay, J.4    Libri, D.5
  • 18
  • 20
    • 64049113602 scopus 로고    scopus 로고
    • Poly(A)-assisted RNA decay and modulators of RNA stability
    • Regnier P, Hajnsdorf E. Poly(A)-assisted RNA decay and modulators of RNA stability. Prog Mol Biol Transl Sci 2009, 85:137-185.
    • (2009) Prog Mol Biol Transl Sci , vol.85 , pp. 137-185
    • Regnier, P.1    Hajnsdorf, E.2
  • 21
    • 0034710943 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions both as a 3′ to 5′ exonuclease and a poly(A) polymerase in Escherichia coli
    • Mohanty BK, Kushner SR. Polynucleotide phosphorylase functions both as a 3′ to 5′ exonuclease and a poly(A) polymerase in Escherichia coli. Proc Natl Acad Sci U S A 2000, 97:11966-11971.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 11966-11971
    • Mohanty, B.K.1    Kushner, S.R.2
  • 22
    • 12344330602 scopus 로고    scopus 로고
    • An important role for RNase R in mRNA decay
    • Cheng ZF, Deutscher MP. An important role for RNase R in mRNA decay. Mol Cell 2005, 17:313-318.
    • (2005) Mol Cell , vol.17 , pp. 313-318
    • Cheng, Z.F.1    Deutscher, M.P.2
  • 23
    • 0026334860 scopus 로고
    • Enzymatic basis for hydrolytic versus phosphorolytic mRNA degradation in Escherichia coli and Bacillus subtilis
    • Deutscher MP, Reuven NB. Enzymatic basis for hydrolytic versus phosphorolytic mRNA degradation in Escherichia coli and Bacillus subtilis. Proc Natl Acad Sci U S A 1991, 88:3277-3280.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 3277-3280
    • Deutscher, M.P.1    Reuven, N.B.2
  • 24
    • 33749072017 scopus 로고    scopus 로고
    • Structural basis for processivity and single-strand specificity of RNase II
    • Zuo Y, Vincent HA, Zhang J, Wang Y, Deutscher MP, Malhotra A. Structural basis for processivity and single-strand specificity of RNase II. Mol Cell 2006, 24:149-156.
    • (2006) Mol Cell , vol.24 , pp. 149-156
    • Zuo, Y.1    Vincent, H.A.2    Zhang, J.3    Wang, Y.4    Deutscher, M.P.5    Malhotra, A.6
  • 25
    • 0037077311 scopus 로고    scopus 로고
    • Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II
    • Cheng ZF, Deutscher MP. Purification and characterization of the Escherichia coli exoribonuclease RNase R. Comparison with RNase II. J Biol Chem 2002, 277:21624-21629.
    • (2002) J Biol Chem , vol.277 , pp. 21624-21629
    • Cheng, Z.F.1    Deutscher, M.P.2
  • 26
    • 33745951483 scopus 로고    scopus 로고
    • Characterization of the functional domains of Escherichia coli RNase II
    • Amblar M, Barbas A, Fialho AM, Arraiano CM. Characterization of the functional domains of Escherichia coli RNase II. J Mol Biol 2006, 360:921-933.
    • (2006) J Mol Biol , vol.360 , pp. 921-933
    • Amblar, M.1    Barbas, A.2    Fialho, A.M.3    Arraiano, C.M.4
  • 27
    • 33749578566 scopus 로고    scopus 로고
    • Substrate recognition and catalysis by the exoribonuclease RNase R
    • Vincent HA, Deutscher MP. Substrate recognition and catalysis by the exoribonuclease RNase R. J Biol Chem 2006, 281:29769-29775.
    • (2006) J Biol Chem , vol.281 , pp. 29769-29775
    • Vincent, H.A.1    Deutscher, M.P.2
  • 28
    • 0033853195 scopus 로고    scopus 로고
    • RNase II removes the oligo(A) tails that destabilize the rpsO mRNA of Escherichia coli
    • Marujo PE, Hajnsdorf E, Le Derout J, Andrade R, Arraiano CM, Regnier P. RNase II removes the oligo(A) tails that destabilize the rpsO mRNA of Escherichia coli. RNA 2000, 6:1185-1193.
    • (2000) RNA , vol.6 , pp. 1185-1193
    • Marujo, P.E.1    Hajnsdorf, E.2    Le Derout, J.3    Andrade, R.4    Arraiano, C.M.5    Regnier, P.6
  • 30
    • 12544252211 scopus 로고    scopus 로고
    • A single mutation in Escherichia coli ribonuclease II inactivates the enzyme without affecting RNA binding
    • Amblar M, Arraiano CM. A single mutation in Escherichia coli ribonuclease II inactivates the enzyme without affecting RNA binding. FEBS J 2005, 272:363-374.
    • (2005) FEBS J , vol.272 , pp. 363-374
    • Amblar, M.1    Arraiano, C.M.2
  • 31
    • 0042858117 scopus 로고    scopus 로고
    • Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus
    • Ishii R, Nureki O, Yokoyama S. Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus. J Biol Chem 2003, 278:32397-32404.
    • (2003) J Biol Chem , vol.278 , pp. 32397-32404
    • Ishii, R.1    Nureki, O.2    Yokoyama, S.3
  • 32
    • 0347683438 scopus 로고    scopus 로고
    • Probing the functional importance of the hexameric ring structure of RNase PH
    • Choi JM, Park EY, Kim JH, Chang SK, Cho Y. Probing the functional importance of the hexameric ring structure of RNase PH. J Biol Chem 2004, 279:755-764.
    • (2004) J Biol Chem , vol.279 , pp. 755-764
    • Choi, J.M.1    Park, E.Y.2    Kim, J.H.3    Chang, S.K.4    Cho, Y.5
  • 33
    • 0026658531 scopus 로고
    • RNase PH is essential for tRNA processing and viability in RNase-deficient Escherichia coli cells
    • Kelly KO, Reuven NB, Li Z, Deutscher MP. RNase PH is essential for tRNA processing and viability in RNase-deficient Escherichia coli cells. J Biol Chem 1992, 267:16015-16018.
    • (1992) J Biol Chem , vol.267 , pp. 16015-16018
    • Kelly, K.O.1    Reuven, N.B.2    Li, Z.3    Deutscher, M.P.4
  • 34
    • 0001486263 scopus 로고
    • Enzymatic synthesis of nucleic acid-like polynucleotides
    • Grunberg-Manago M, Oritz PJ, Ochoa S. Enzymatic synthesis of nucleic acid-like polynucleotides. Science 1955, 122:907-910.
    • (1955) Science , vol.122 , pp. 907-910
    • Grunberg-Manago, M.1    Oritz, P.J.2    Ochoa, S.3
  • 36
    • 0004574825 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase.
    • Creighton TE, ed. New York: John Willy & Sons, Inc.;
    • Littauer UZ, Grunberg-Manago M. Polynucleotide phosphorylase. In: Creighton TE, ed. The Encyclopedia of Molecular Biology. New York: John Willy & Sons, Inc.; 1999, 1911-1918.
    • (1999) The Encyclopedia of Molecular Biology. , pp. 1911-1918
    • Littauer, U.Z.1    Grunberg-Manago, M.2
  • 37
    • 0033368475 scopus 로고    scopus 로고
    • Messenger RNA stability and its role in control of gene expression in bacteria and phages
    • Grunberg-Manago M. Messenger RNA stability and its role in control of gene expression in bacteria and phages. Annu Rev Genet 1999, 33:193-227.
    • (1999) Annu Rev Genet , vol.33 , pp. 193-227
    • Grunberg-Manago, M.1
  • 38
    • 7044285063 scopus 로고    scopus 로고
    • The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli
    • Mohanty BK, Maples VF, Kushner SR. The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli. Mol Microbiol 2004, 54:905-920.
    • (2004) Mol Microbiol , vol.54 , pp. 905-920
    • Mohanty, B.K.1    Maples, V.F.2    Kushner, S.R.3
  • 39
    • 0035793043 scopus 로고    scopus 로고
    • RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E
    • Liou GG, Jane WN, Cohen SN, Lin NS, Lin-Chao S. RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E. Proc Natl Acad Sci U S A 2001, 98:63-68.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 63-68
    • Liou, G.G.1    Jane, W.N.2    Cohen, S.N.3    Lin, N.S.4    Lin-Chao, S.5
  • 41
    • 0032617132 scopus 로고    scopus 로고
    • Degradation of mRNA in Escherichia coli: an old problem with some new twists
    • Coburn GA, Mackie GA. Degradation of mRNA in Escherichia coli: an old problem with some new twists. Prog Nucleic Acid Res Mol Biol 1999, 62:55-108.
    • (1999) Prog Nucleic Acid Res Mol Biol , vol.62 , pp. 55-108
    • Coburn, G.A.1    Mackie, G.A.2
  • 42
    • 0242400018 scopus 로고    scopus 로고
    • Degradation of mRNA in bacteria: emergence of ubiquitous features
    • Regnier P, Arraiano CM. Degradation of mRNA in bacteria: emergence of ubiquitous features. Bioessays 2000, 22:235-244.
    • (2000) Bioessays , vol.22 , pp. 235-244
    • Regnier, P.1    Arraiano, C.M.2
  • 43
    • 35548995356 scopus 로고    scopus 로고
    • The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E
    • Carpousis AJ. The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E. Annu Rev Microbiol 2007, 61:71-87
    • (2007) Annu Rev Microbiol , vol.61 , pp. 71-87
    • Carpousis, A.J.1
  • 45
    • 0037174922 scopus 로고    scopus 로고
    • DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E
    • Liou GG, Chang HY, Lin CS, Lin-Chao S. DEAD box RhlB RNA helicase physically associates with exoribonuclease PNPase to degrade double-stranded RNA independent of the degradosome-assembling region of RNase E. J Biol Chem 2002, 277:41157-41162.
    • (2002) J Biol Chem , vol.277 , pp. 41157-41162
    • Liou, G.G.1    Chang, H.Y.2    Lin, C.S.3    Lin-Chao, S.4
  • 47
    • 64049109732 scopus 로고    scopus 로고
    • RNA polyadenylation and decay in mitochondria and chloroplasts
    • Schuster G, Stern D. RNA polyadenylation and decay in mitochondria and chloroplasts. Prog Mol Biol Transl Sci 2009, 85:393-422.
    • (2009) Prog Mol Biol Transl Sci , vol.85 , pp. 393-422
    • Schuster, G.1    Stern, D.2
  • 48
    • 0037168641 scopus 로고    scopus 로고
    • Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35, in the context of terminal differentiation and cellular senescence
    • Leszczyniecka M, Kang DC, Sarkar D, Su ZZ, Holmes M, Valerie K, Fisher PB. Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35, in the context of terminal differentiation and cellular senescence. Proc Natl Acad Sci U S A 2002, 99:16636-16641.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16636-16641
    • Leszczyniecka, M.1    Kang, D.C.2    Sarkar, D.3    Su, Z.Z.4    Holmes, M.5    Valerie, K.6    Fisher, P.B.7
  • 49
    • 0041589211 scopus 로고    scopus 로고
    • Down-regulation of Myc as a potential target for growth arrest induced by human polynucleotide phosphorylase (hPNPaseold-35) in human melanoma cells
    • Sarkar D, Leszczyniecka M, Kang DC, Lebedeva IV, Valerie K, Dhar S, Pandita TK, Fisher PB. Down-regulation of Myc as a potential target for growth arrest induced by human polynucleotide phosphorylase (hPNPaseold-35) in human melanoma cells. J Biol Chem 2003, 278:24542-24551.
    • (2003) J Biol Chem , vol.278 , pp. 24542-24551
    • Sarkar, D.1    Leszczyniecka, M.2    Kang, D.C.3    Lebedeva, I.V.4    Valerie, K.5    Dhar, S.6    Pandita, T.K.7    Fisher, P.B.8
  • 50
    • 23344451161 scopus 로고    scopus 로고
    • Defining the domains of human polynucleotide phosphorylase (hPNPaseOLD-35) mediating cellular senescence
    • Sarkar D, Park ES, Emdad L, Randolph A, Valerie K, Fisher PB. Defining the domains of human polynucleotide phosphorylase (hPNPaseOLD-35) mediating cellular senescence. Mol Cell Biol 2005, 25:7333-7343.
    • (2005) Mol Cell Biol , vol.25 , pp. 7333-7343
    • Sarkar, D.1    Park, E.S.2    Emdad, L.3    Randolph, A.4    Valerie, K.5    Fisher, P.B.6
  • 51
    • 0034934778 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts
    • Yehudai-Resheff S, Hirsh M, Schuster G. Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts. Mol Cell Biol 2001, 21:5408-5416.
    • (2001) Mol Cell Biol , vol.21 , pp. 5408-5416
    • Yehudai-Resheff, S.1    Hirsh, M.2    Schuster, G.3
  • 53
    • 33750986200 scopus 로고    scopus 로고
    • A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space
    • Rainey RN, Glavin JD, Chen HW, French SW, Teitell MA, Koehler CM. A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space. Mol Cell Biol 2006, 26:8488-8497.
    • (2006) Mol Cell Biol , vol.26 , pp. 8488-8497
    • Rainey, R.N.1    Glavin, J.D.2    Chen, H.W.3    French, S.W.4    Teitell, M.A.5    Koehler, C.M.6
  • 54
    • 36249001217 scopus 로고    scopus 로고
    • Human polynucleotide phosphorylase: location matters
    • Chen HW, Koehler CM, Teitell MA. Human polynucleotide phosphorylase: location matters. Trends Cell Biol 2007, 17:600-608.
    • (2007) Trends Cell Biol , vol.17 , pp. 600-608
    • Chen, H.W.1    Koehler, C.M.2    Teitell, M.A.3
  • 55
    • 38649100934 scopus 로고    scopus 로고
    • Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts
    • Portnoy V, Palnizky G, Yehudai-Resheff S, Glaser F, Schuster G. Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts. RNA 2008, 14:297-309.
    • (2008) RNA , vol.14 , pp. 297-309
    • Portnoy, V.1    Palnizky, G.2    Yehudai-Resheff, S.3    Glaser, F.4    Schuster, G.5
  • 56
    • 38649115643 scopus 로고    scopus 로고
    • Stable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNA
    • Slomovic S, Schuster G. Stable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNA. RNA 2008, 14:310-323.
    • (2008) RNA , vol.14 , pp. 310-323
    • Slomovic, S.1    Schuster, G.2
  • 58
    • 0036977391 scopus 로고    scopus 로고
    • Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring
    • Raijmakers R, Egberts WV, van Venrooij WJ, Pruijn GJ. Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring. J Mol Biol 2002, 323:653-663.
    • (2002) J Mol Biol , vol.323 , pp. 653-663
    • Raijmakers, R.1    Egberts, W.V.2    van Venrooij, W.J.3    Pruijn, G.J.4
  • 59
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
    • Symmons MF, Jones GH, Luisi BF. A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Structure 2000, 8:1215-1226.
    • (2000) Structure , vol.8 , pp. 1215-1226
    • Symmons, M.F.1    Jones, G.H.2    Luisi, B.F.3
  • 60
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: structural analysis and phylogenetic distribution
    • Zuo Y, Deutscher MP. 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
  • 61
    • 0141453035 scopus 로고    scopus 로고
    • Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins
    • Yehudai-Resheff S, Portnoy V, Yogev S, Adir N, Schuster G. Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins. Plant Cell 2003, 15:2003-2019.
    • (2003) Plant Cell , vol.15 , pp. 2003-2019
    • Yehudai-Resheff, S.1    Portnoy, V.2    Yogev, S.3    Adir, N.4    Schuster, G.5
  • 62
    • 0036382938 scopus 로고    scopus 로고
    • Mutational analysis of polynucleotide phosphorylase from Escherichia coli
    • Jarrige A, Brechemier-Baey D, Mathy N, Duche O, Portier C. Mutational analysis of polynucleotide phosphorylase from Escherichia coli. J Mol Biol 2002, 321:397-409.
    • (2002) J Mol Biol , vol.321 , pp. 397-409
    • Jarrige, A.1    Brechemier-Baey, D.2    Mathy, N.3    Duche, O.4    Portier, C.5
  • 63
    • 67349257830 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly
    • Nurmohamed S, Vaidialingam B, Callaghan AJ, Luisi BF. Crystal structure of Escherichia coli polynucleotide phosphorylase core bound to RNase E, RNA and manganese: implications for catalytic mechanism and RNA degradosome assembly. J Mol Biol 2009, 389:17-33.
    • (2009) J Mol Biol , vol.389 , pp. 17-33
    • Nurmohamed, S.1    Vaidialingam, B.2    Callaghan, A.J.3    Luisi, B.F.4
  • 64
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′ to 5′ exoribonucleases
    • Mitchel P, Petfalski E, Shevchenko A, Mann M, Tollervey D. The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′ to 5′ exoribonucleases. Cell 1997, 91:457-466.
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchel, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 65
    • 0032727868 scopus 로고    scopus 로고
    • The exosome: a proteasome for RNA?
    • van Hoof A, Parker R. The exosome: a proteasome for RNA? Cell 1999, 99:347-350.
    • (1999) Cell , vol.99 , pp. 347-350
    • van Hoof, A.1    Parker, R.2
  • 66
    • 4344573414 scopus 로고    scopus 로고
    • The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm
    • Raijmakers R, Schilders G, Pruijn GJ. The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm. Eur J Cell Biol 2004, 83:175-183.
    • (2004) Eur J Cell Biol , vol.83 , pp. 175-183
    • Raijmakers, R.1    Schilders, G.2    Pruijn, G.J.3
  • 68
    • 33748510412 scopus 로고    scopus 로고
    • The exosome: a macromolecular cage for controlled RNA degradation
    • Buttner K, Wenig K, Hopfner KP. The exosome: a macromolecular cage for controlled RNA degradation. Mol Microbiol 2006, 61:1372-1379.
    • (2006) Mol Microbiol , vol.61 , pp. 1372-1379
    • Buttner, K.1    Wenig, K.2    Hopfner, K.P.3
  • 69
    • 0036464532 scopus 로고    scopus 로고
    • Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3′ → 5′ exonuclease containing S1 and KH RNA-binding domains
    • Chekanova JA, Dutko JA, Mian IS, Belostotsky DA. Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3′ → 5′ exonuclease containing S1 and KH RNA-binding domains. Nucleic Acids Res 2002, 30:695-700.
    • (2002) Nucleic Acids Res , vol.30 , pp. 695-700
    • Chekanova, J.A.1    Dutko, J.A.2    Mian, I.S.3    Belostotsky, D.A.4
  • 70
    • 0035898660 scopus 로고    scopus 로고
    • The exosome of Trypanosoma brucei
    • Estevez AM, Kempf T, Clayton C. The exosome of Trypanosoma brucei. EMBO J 2001, 20:3831-3839.
    • (2001) EMBO J , vol.20 , pp. 3831-3839
    • Estevez, A.M.1    Kempf, T.2    Clayton, C.3
  • 72
    • 3543111496 scopus 로고    scopus 로고
    • A protein interaction framework for human mRNA degradation
    • Lehner B, Sanderson CM. A protein interaction framework for human mRNA degradation. Genome Res 2004, 14:1315-1323.
    • (2004) Genome Res , vol.14 , pp. 1315-1323
    • Lehner, B.1    Sanderson, C.M.2
  • 73
    • 33845407784 scopus 로고    scopus 로고
    • Reconstitution, activities, and structure of the eukaryotic RNA exosome
    • Liu Q, Greimann JC, Lima CD. Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 2006, 127:1223-1237.
    • (2006) Cell , vol.127 , pp. 1223-1237
    • Liu, Q.1    Greimann, J.C.2    Lima, C.D.3
  • 74
    • 33846068920 scopus 로고    scopus 로고
    • A single subunit, Dis3, is essentially responsible for yeast exosome core activity
    • Dziembowski A, Lorentzen E, Conti E, Seraphin B. A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat Struct Mol Biol 2007, 14:15-22.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 15-22
    • Dziembowski, A.1    Lorentzen, E.2    Conti, E.3    Seraphin, B.4
  • 76
    • 27644496002 scopus 로고    scopus 로고
    • Structural basis of 3′ end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core
    • Lorentzen E, Conti E. Structural basis of 3′ end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core. Mol Cell 2005, 20:473-481.
    • (2005) Mol Cell , vol.20 , pp. 473-481
    • Lorentzen, E.1    Conti, E.2
  • 77
    • 33646523370 scopus 로고    scopus 로고
    • The exosome and the proteasome: nano-compartments for degradation
    • Lorentzen E, Conti E. The exosome and the proteasome: nano-compartments for degradation. Cell 2006, 125:651-654.
    • (2006) Cell , vol.125 , pp. 651-654
    • Lorentzen, E.1    Conti, E.2
  • 78
    • 28544443737 scopus 로고    scopus 로고
    • RNA polyadenylation in archaea: not observed in Haloferax while the exosome polyadenylates RNA in Sulfolobus
    • Portnoy V, Evguenieva-Hackenberg E, Klein F, Walter P, Lorentzen E, Klug G, Schuster G. RNA polyadenylation in archaea: not observed in Haloferax while the exosome polyadenylates RNA in Sulfolobus. EMBO Rep 2005, 6:1188-1193.
    • (2005) EMBO Rep , vol.6 , pp. 1188-1193
    • Portnoy, V.1    Evguenieva-Hackenberg, E.2    Klein, F.3    Walter, P.4    Lorentzen, E.5    Klug, G.6    Schuster, G.7
  • 79
    • 27644435644 scopus 로고    scopus 로고
    • Structural framework for the mechanism of archaeal exosomes in RNA processing
    • Buttner K, Wenig K, Hopfner KP. Structural framework for the mechanism of archaeal exosomes in RNA processing. Mol Cell 2005, 20:461-471.
    • (2005) Mol Cell , vol.20 , pp. 461-471
    • Buttner, K.1    Wenig, K.2    Hopfner, K.P.3
  • 80
    • 33845606715 scopus 로고    scopus 로고
    • RNA polyadenylation and degradation in different archaea; roles of the exosome and RNase R
    • Portnoy V, Schuster G. RNA polyadenylation and degradation in different archaea; roles of the exosome and RNase R. Nucleic Acids Res 2006, 34:5923-5931.
    • (2006) Nucleic Acids Res , vol.34 , pp. 5923-5931
    • Portnoy, V.1    Schuster, G.2
  • 81
    • 0034745504 scopus 로고    scopus 로고
    • Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach
    • Koonin EV, Wolf YI, Aravind L. Prediction of the archaeal exosome and its connections with the proteasome and the translation and transcription machineries by a comparative-genomic approach. Genome Res 2001, 11:240-252.
    • (2001) Genome Res , vol.11 , pp. 240-252
    • Koonin, E.V.1    Wolf, Y.I.2    Aravind, L.3
  • 84
    • 62049085366 scopus 로고    scopus 로고
    • The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome
    • Schneider C, Leung E, Brown J, Tollervey D. The N-terminal PIN domain of the exosome subunit Rrp44 harbors endonuclease activity and tethers Rrp44 to the yeast core exosome. Nucleic Acids Res 2009, 37:1127-1140.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1127-1140
    • Schneider, C.1    Leung, E.2    Brown, J.3    Tollervey, D.4
  • 85
    • 57749189164 scopus 로고    scopus 로고
    • Endonucleolytic RNA cleavage by a eukaryotic exosome
    • Lebreton A, Tomecki R, Dziembowski A, Seraphin B. Endonucleolytic RNA cleavage by a eukaryotic exosome. Nature 2008, 456:993-996.
    • (2008) Nature , vol.456 , pp. 993-996
    • Lebreton, A.1    Tomecki, R.2    Dziembowski, A.3    Seraphin, B.4
  • 86
    • 70350336247 scopus 로고    scopus 로고
    • The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation
    • Bonneau F, Basquin J, Ebert J, Lorentzen E, Conti E. The yeast exosome functions as a macromolecular cage to channel RNA substrates for degradation. Cell 2009, 139:547-559.
    • (2009) Cell , vol.139 , pp. 547-559
    • Bonneau, F.1    Basquin, J.2    Ebert, J.3    Lorentzen, E.4    Conti, E.5
  • 87
    • 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 MW, Burkard KT, Butler JS. 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    Burkard, K.T.2    Butler, J.S.3
  • 91
    • 34548712987 scopus 로고    scopus 로고
    • The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein
    • Stead JA, Costello JL, Livingstone MJ, Mitchell P. The PMC2NT domain of the catalytic exosome subunit Rrp6p provides the interface for binding with its cofactor Rrp47p, a nucleic acid-binding protein. Nucleic Acids Res 2007, 35:5556-5567.
    • (2007) Nucleic Acids Res , vol.35 , pp. 5556-5567
    • Stead, J.A.1    Costello, J.L.2    Livingstone, M.J.3    Mitchell, P.4
  • 92
    • 50249112157 scopus 로고    scopus 로고
    • A yeast exosome cofactor, Mpp6, functions in RNA surveillance and in the degradation of noncoding RNA transcripts
    • Milligan L, Decourty L, Saveanu C, Rappsilber J, Ceulemans H, Jacquier A, Tollervey D. A yeast exosome cofactor, Mpp6, functions in RNA surveillance and in the degradation of noncoding RNA transcripts. Mol Cell Biol 2008, 28:5446-5457.
    • (2008) Mol Cell Biol , vol.28 , pp. 5446-5457
    • Milligan, L.1    Decourty, L.2    Saveanu, C.3    Rappsilber, J.4    Ceulemans, H.5    Jacquier, A.6    Tollervey, D.7
  • 93
    • 29244475356 scopus 로고    scopus 로고
    • MPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA maturation
    • Schilders G, Raijmakers R, Raats JM, Pruijn GJ. MPP6 is an exosome-associated RNA-binding protein involved in 5.8S rRNA maturation. Nucleic Acids Res 2005, 33:6795-6804.
    • (2005) Nucleic Acids Res , vol.33 , pp. 6795-6804
    • Schilders, G.1    Raijmakers, R.2    Raats, J.M.3    Pruijn, G.J.4
  • 94
    • 34250888278 scopus 로고    scopus 로고
    • Human cell growth requires a functional cytoplasmic exosome, which is involved in various mRNA decay pathways
    • van Dijk EL, Schilders G, Pruijn GJ. Human cell growth requires a functional cytoplasmic exosome, which is involved in various mRNA decay pathways. RNA 2007, 13:1027-1035.
    • (2007) RNA , vol.13 , pp. 1027-1035
    • van Dijk, E.L.1    Schilders, G.2    Pruijn, G.J.3
  • 95
    • 0031000662 scopus 로고    scopus 로고
    • RNase E: still a wonderfully mysterious enzyme
    • Cohen SN, McDowall KJ. RNase E: still a wonderfully mysterious enzyme. Mol Microbiol 1997, 23:1099-1106.
    • (1997) Mol Microbiol , vol.23 , pp. 1099-1106
    • Cohen, S.N.1    McDowall, K.J.2
  • 96
    • 0036719292 scopus 로고    scopus 로고
    • mRNA decay in Escherichia coli comes of age
    • Kushner SR. mRNA decay in Escherichia coli comes of age. J Bacteriol 2002, 184:4658-4665.
    • (2002) J Bacteriol , vol.184 , pp. 4658-4665
    • Kushner, S.R.1
  • 97
    • 34250729202 scopus 로고    scopus 로고
    • Maturation and degradation of RNA in bacteria
    • Condon C. Maturation and degradation of RNA in bacteria. Curr Opin Microbiol 2007, 10:271-278.
    • (2007) Curr Opin Microbiol , vol.10 , pp. 271-278
    • Condon, C.1
  • 98
    • 32644435694 scopus 로고    scopus 로고
    • Degradation of RNA in bacteria: comparison of mRNA and stable RNA
    • Deutscher MP. Degradation of RNA in bacteria: comparison of mRNA and stable RNA. Nucleic Acids Res 2006, 34:659-666.
    • (2006) Nucleic Acids Res , vol.34 , pp. 659-666
    • Deutscher, M.P.1
  • 99
    • 33846946171 scopus 로고    scopus 로고
    • Information available at cut rates: structure and mechanism of ribonucleases
    • Worrall JA, Luisi BF. Information available at cut rates: structure and mechanism of ribonucleases. Curr Opin Struct Biol 2007, 17:128-137.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 128-137
    • Worrall, J.A.1    Luisi, B.F.2
  • 101
    • 0038182527 scopus 로고    scopus 로고
    • RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli
    • Rott R, Zipor G, Portnoy V, Liveanu V, Schuster G. RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli. J Biol Chem 2003, 278:15771-15777.
    • (2003) J Biol Chem , vol.278 , pp. 15771-15777
    • Rott, R.1    Zipor, G.2    Portnoy, V.3    Liveanu, V.4    Schuster, G.5
  • 102
    • 0038687705 scopus 로고    scopus 로고
    • A Streptomyces coelicolor functional orthologue of Escherichia coli RNase E shows shuffling of catalytic and PNPase-binding domains
    • Lee K, Cohen SN. A Streptomyces coelicolor functional orthologue of Escherichia coli RNase E shows shuffling of catalytic and PNPase-binding domains. Mol Microbiol 2003, 48:349-360.
    • (2003) Mol Microbiol , vol.48 , pp. 349-360
    • Lee, K.1    Cohen, S.N.2
  • 104
    • 38349117689 scopus 로고    scopus 로고
    • The bacterial enzyme RppH triggers messenger RNA degradation by 5′ pyrophosphate removal
    • Deana A, Celesnik H, Belasco JG. The bacterial enzyme RppH triggers messenger RNA degradation by 5′ pyrophosphate removal. Nature 2008, 451:355-358.
    • (2008) Nature , vol.451 , pp. 355-358
    • Deana, A.1    Celesnik, H.2    Belasco, J.G.3
  • 105
  • 106
    • 70450222923 scopus 로고    scopus 로고
    • RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis
    • Shahbabian K, Jamalli A, Zig L, Putzer H. RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis. EMBO J 2009, 28:3523-3533.
    • (2009) EMBO J , vol.28 , pp. 3523-3533
    • Shahbabian, K.1    Jamalli, A.2    Zig, L.3    Putzer, H.4
  • 107
    • 17844361922 scopus 로고    scopus 로고
    • Ribonucleases J1 and J2: two novel endoribonucleases in B.subtilis with functional homology to E.coli RNase E
    • Even S, Pellegrini O, Zig L, Labas V, Vinh J, Brechemmier-Baey D, Putzer H. Ribonucleases J1 and J2: two novel endoribonucleases in B.subtilis with functional homology to E.coli RNase E. Nucleic Acids Res 2005, 33:2141-2152.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2141-2152
    • Even, S.1    Pellegrini, O.2    Zig, L.3    Labas, V.4    Vinh, J.5    Brechemmier-Baey, D.6    Putzer, H.7
  • 109
    • 70350374351 scopus 로고    scopus 로고
    • Bacillus subtilis trp leader RNA: Specificity of RNase J1 endonuclease cleavage and PNPase processing
    • Deikus G, Bechhofer DH. Bacillus subtilis trp leader RNA: Specificity of RNase J1 endonuclease cleavage and PNPase processing. J Biol Chem 2009, 284:26394-401.
    • (2009) J Biol Chem , vol.284 , pp. 26394-26401
    • Deikus, G.1    Bechhofer, D.H.2
  • 110
    • 47749143603 scopus 로고    scopus 로고
    • Role of Bacillus subtilis RNase J1 endonuclease and 5′ exonuclease activities in trp leader RNA turnover
    • Deikus G, Condon C, Bechhofer DH. Role of Bacillus subtilis RNase J1 endonuclease and 5′ exonuclease activities in trp leader RNA turnover. J Biol Chem 2008, 283:17158-87.
    • (2008) J Biol Chem , vol.283 , pp. 17158-17187
    • Deikus, G.1    Condon, C.2    Bechhofer, D.H.3
  • 111
    • 34249101864 scopus 로고    scopus 로고
    • 5′-to-3′ exoribonuclease activity in bacteria: role of RNase J1 in rRNA maturation and 5′ stability of mRNA
    • Mathy N, Benard L, Pellegrini O, Daou R, Wen T, Condon C. 5′-to-3′ exoribonuclease activity in bacteria: role of RNase J1 in rRNA maturation and 5′ stability of mRNA. Cell 2007, 129:681-692.
    • (2007) Cell , vol.129 , pp. 681-692
    • Mathy, N.1    Benard, L.2    Pellegrini, O.3    Daou, R.4    Wen, T.5    Condon, C.6
  • 114
    • 77952170843 scopus 로고    scopus 로고
    • Addition of poly(A) and poly(A)-rich tails during RNA degradation in the cytoplasm of human cells
    • Slomovic S, Fremder E, Staals RH, Pruijn GJ, Schuster G. Addition of poly(A) and poly(A)-rich tails during RNA degradation in the cytoplasm of human cells. Proc Natl Acad Sci U S A 2010, 107:7407-7412.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 7407-7412
    • Slomovic, S.1    Fremder, E.2    Staals, R.H.3    Pruijn, G.J.4    Schuster, G.5
  • 115
    • 21844443073 scopus 로고    scopus 로고
    • Addition of poly(A) and heteropolymeric 3′ ends in Bacillus subtilis wild-type and polynucleotide phosphorylase-deficient strains
    • Campos-Guillen J, Bralley P, Jones GH, Bechhofer DH, Olmedo-Alvarez G. Addition of poly(A) and heteropolymeric 3′ ends in Bacillus subtilis wild-type and polynucleotide phosphorylase-deficient strains. J Bacteriol 2005, 187:4698-4706.
    • (2005) J Bacteriol , vol.187 , pp. 4698-4706
    • Campos-Guillen, J.1    Bralley, P.2    Jones, G.H.3    Bechhofer, D.H.4    Olmedo-Alvarez, G.5
  • 116
    • 0033009854 scopus 로고    scopus 로고
    • Prochlorococcus, a marine photosynthetic prokaryote of global significance
    • Partensky F, Hess WR, Vaulot D. Prochlorococcus, a marine photosynthetic prokaryote of global significance. Microbiol Mol Biol Rev 1999, 63:106-127.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 106-127
    • Partensky, F.1    Hess, W.R.2    Vaulot, D.3
  • 117
    • 42649140571 scopus 로고    scopus 로고
    • Mycoplasma gallisepticum as the first analyzed bacterium in which RNA is not polyadenylated
    • Portnoy V, Schuster G. Mycoplasma gallisepticum as the first analyzed bacterium in which RNA is not polyadenylated. FEMS Microbiol Lett 2008, 283:97-103.
    • (2008) FEMS Microbiol Lett , vol.283 , pp. 97-103
    • Portnoy, V.1    Schuster, G.2
  • 118
    • 67649476386 scopus 로고    scopus 로고
    • Polyadenylation in Arabidopsis and Chlamydomonas organelles: the input of nucleotidyltransferases, poly(A) polymerases and polynucleotide phosphorylase
    • Zimmer SL, Schein A, Zipor G, Stern DB, Schuster G. Polyadenylation in Arabidopsis and Chlamydomonas organelles: the input of nucleotidyltransferases, poly(A) polymerases and polynucleotide phosphorylase. Plant J 2009, 59:88-99.
    • (2009) Plant J , vol.59 , pp. 88-99
    • Zimmer, S.L.1    Schein, A.2    Zipor, G.3    Stern, D.B.4    Schuster, G.5
  • 119
    • 0033199033 scopus 로고    scopus 로고
    • 5′ to 3′ exoribonucleolytic activity is a normal component of chloroplast mRNA decay pathways
    • Drager RG, Higgs DC, Kindle KL, Stern DB. 5′ to 3′ exoribonucleolytic activity is a normal component of chloroplast mRNA decay pathways. Plant J 1999, 19:521-531.
    • (1999) Plant J , vol.19 , pp. 521-531
    • Drager, R.G.1    Higgs, D.C.2    Kindle, K.L.3    Stern, D.B.4
  • 120
    • 0031910348 scopus 로고    scopus 로고
    • In vivo evidence for 5′ → 3′ exoribonuclease degradation of an unstable chloroplast mRNA
    • Drager RG, Girard-Bascou J, Choquet Y, Kindle KL, Stern DB. In vivo evidence for 5′ → 3′ exoribonuclease degradation of an unstable chloroplast mRNA. Plant J 1998, 13:85-96.
    • (1998) Plant J , vol.13 , pp. 85-96
    • Drager, R.G.1    Girard-Bascou, J.2    Choquet, Y.3    Kindle, K.L.4    Stern, D.B.5
  • 121
    • 69449096380 scopus 로고    scopus 로고
    • Polyadenylation-assisted RNA degradation processes in plants
    • Lange H, Sement FM, Canaday J, Gagliardi D. Polyadenylation-assisted RNA degradation processes in plants. Trends Plant Sci 2009, 14:497-504.
    • (2009) Trends Plant Sci , vol.14 , pp. 497-504
    • Lange, H.1    Sement, F.M.2    Canaday, J.3    Gagliardi, D.4
  • 122
    • 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 TE, Marzluff WF. 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
  • 123
    • 40549087668 scopus 로고    scopus 로고
    • Molecular biology. A tail tale for U
    • Wickens M, Kwak JE. Molecular biology. A tail tale for U. Science 2008, 319:1344-1345.
    • (2008) Science , vol.319 , pp. 1344-1345
    • Wickens, M.1    Kwak, J.E.2
  • 124
    • 34249026025 scopus 로고    scopus 로고
    • A family of poly(U) polymerases
    • Kwak JE, Wickens M. A family of poly(U) polymerases. RNA 2007, 13:860-867.
    • (2007) RNA , vol.13 , pp. 860-867
    • Kwak, J.E.1    Wickens, M.2
  • 125
    • 66849122924 scopus 로고    scopus 로고
    • Decapping is preceded by 3′ uridylation in a novel pathway of bulk mRNA turnover
    • Rissland OS, Norbury CJ. 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
  • 127
    • 0037449772 scopus 로고    scopus 로고
    • The yeast mitochondrial degradosome. Its composition, interplay between RNA helicase and RNase activities and the role in mitochondrial RNA metabolism
    • Dziembowski A, Piwowarski J, Hoser R, Minczuk M, Dmochowska A, Siep M, van der Spek H, Grivell L, Stepien PP. The yeast mitochondrial degradosome. Its composition, interplay between RNA helicase and RNase activities and the role in mitochondrial RNA metabolism. J Biol Chem 2003, 278:1603-1611.
    • (2003) J Biol Chem , vol.278 , pp. 1603-1611
    • Dziembowski, A.1    Piwowarski, J.2    Hoser, R.3    Minczuk, M.4    Dmochowska, A.5    Siep, M.6    van der Spek, H.7    Grivell, L.8    Stepien, P.P.9
  • 128
    • 0037371743 scopus 로고    scopus 로고
    • Uridine insertion/deletion RNA editing in trypanosome mitochondria: a complex business
    • Simpson L, Sbicego S, Aphasizhev R. Uridine insertion/deletion RNA editing in trypanosome mitochondria: a complex business. RNA 2003, 9:265-276.
    • (2003) RNA , vol.9 , pp. 265-276
    • Simpson, L.1    Sbicego, S.2    Aphasizhev, R.3
  • 129
    • 14044264228 scopus 로고    scopus 로고
    • Opposing effects of polyadenylation on the stability of edited and unedited mitochondrial RNAs in Trypanosoma brucei
    • Kao CY, Read LK. Opposing effects of polyadenylation on the stability of edited and unedited mitochondrial RNAs in Trypanosoma brucei. Mol Cell Biol 2005, 25:1634-1644.
    • (2005) Mol Cell Biol , vol.25 , pp. 1634-1644
    • Kao, C.Y.1    Read, L.K.2
  • 130
    • 44649128170 scopus 로고    scopus 로고
    • 3′ adenylation determines mRNA abundance and monitors completion of RNA editing in T. brucei mitochondria
    • Etheridge RD, Aphasizheva I, Gershon PD, Aphasizhev R. 3′ adenylation determines mRNA abundance and monitors completion of RNA editing in T. brucei mitochondria. EMBO J 2008, 27:1596-1608.
    • (2008) EMBO J , vol.27 , pp. 1596-1608
    • Etheridge, R.D.1    Aphasizheva, I.2    Gershon, P.D.3    Aphasizhev, R.4
  • 131
    • 34447262522 scopus 로고    scopus 로고
    • Targeted depletion of a mitochondrial nucleotidyltransferase suggests the presence of multiple enzymes that polymerize mRNA 3′ tails in Trypanosoma brucei mitochondria
    • Kao CY, Read LK. Targeted depletion of a mitochondrial nucleotidyltransferase suggests the presence of multiple enzymes that polymerize mRNA 3′ tails in Trypanosoma brucei mitochondria. Mol Biochem Parasitol 2007, 154:158-169.
    • (2007) Mol Biochem Parasitol , vol.154 , pp. 158-169
    • Kao, C.Y.1    Read, L.K.2
  • 132
    • 0019444843 scopus 로고
    • tRNA punctuation model of RNA processing in human mitochondria
    • Ojala D, Montoya J, Attardi G. tRNA punctuation model of RNA processing in human mitochondria. Nature 1981, 290:470-474.
    • (1981) Nature , vol.290 , pp. 470-474
    • Ojala, D.1    Montoya, J.2    Attardi, G.3
  • 133
    • 54549088876 scopus 로고    scopus 로고
    • RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
    • Holzmann J, Frank P, Loffler E, Bennett K, Gerner C, Rossmanith W. RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell 2008, 135:462-474.
    • (2008) Cell , vol.135 , pp. 462-474
    • Holzmann, J.1    Frank, P.2    Loffler, E.3    Bennett, K.4    Gerner, C.5    Rossmanith, W.6
  • 135
    • 21244454028 scopus 로고    scopus 로고
    • Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase
    • Nagaike T, Suzuki T, Katoh T, Ueda T. Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase. J Biol Chem 2005, 280:19721-19727.
    • (2005) J Biol Chem , vol.280 , pp. 19721-19727
    • Nagaike, T.1    Suzuki, T.2    Katoh, T.3    Ueda, T.4
  • 136
    • 60549114880 scopus 로고    scopus 로고
    • Widespread bidirectional promoters are the major source of cryptic transcripts in yeast
    • Neil H, Malabat C, d'Aubenton-Carafa Y, Xu Z, Steinmetz LM, Jacquier A. Widespread bidirectional promoters are the major source of cryptic transcripts in yeast. Nature 2009, 457:1038-1042.
    • (2009) Nature , vol.457 , pp. 1038-1042
    • Neil, H.1    Malabat, C.2    d'Aubenton-Carafa, Y.3    Xu, Z.4    Steinmetz, L.M.5    Jacquier, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.