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Volumn 1779, Issue 4, 2008, Pages 247-255

Polynucleotide phosphorylase and the archaeal exosome as poly(A)-polymerases

Author keywords

Exosome; Heteropolymeric tails; PNPase; RNA degradation; RNA polyadenylation

Indexed keywords

DNA DIRECTED DNA POLYMERASE ALPHA; HISTONE; POLYADENYLATED RNA; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE;

EID: 41549120528     PISSN: 18749399     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2007.12.004     Document Type: Review
Times cited : (54)

References (74)
  • 1
    • 0001486263 scopus 로고
    • Enzymatic synthesis of nucleic acidlike polynucleotides
    • Grunberg-Manago M., Oritz P.J., and Ochoa S. Enzymatic synthesis of nucleic acidlike polynucleotides. Science 122 (1955) 907-910
    • (1955) Science , vol.122 , pp. 907-910
    • Grunberg-Manago, M.1    Oritz, P.J.2    Ochoa, S.3
  • 4
    • 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. 33 (1999) 193-227
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 193-227
    • Grunberg-Manago, M.1
  • 5
    • 0034710943 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions both as a 3′ to 5′ exonuclease and a poly(A) polymerase in Escherichia coli
    • Mohanty B.K., and Kushner S.R. 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. 97 (2000) 11966-11971
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 11966-11971
    • Mohanty, B.K.1    Kushner, S.R.2
  • 6
    • 0035193362 scopus 로고    scopus 로고
    • Exoribonucleases and their multiple roles in RNA metabolism
    • Deutscher M.P., and Li Z. Exoribonucleases and their multiple roles in RNA metabolism. Prog. Nucleic Acid Res. Mol. Biol. 66 (2001) 67-105
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.66 , pp. 67-105
    • Deutscher, M.P.1    Li, Z.2
  • 7
    • 35548995356 scopus 로고    scopus 로고
    • The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E
    • Carpousis A.J. The RNA degradosome of Escherichia coli: an mRNA-degrading machine assembled on RNase E. Annu. Rev. Microbiol. 61 (2007) 71-87
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 71-87
    • Carpousis, A.J.1
  • 8
    • 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., and Schuster G. Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts. Mol. Cell. Biol. 21 (2001) 5408-5416
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5408-5416
    • Yehudai-Resheff, S.1    Hirsh, M.2    Schuster, G.3
  • 9
    • 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., and Schuster G. RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli. J. Biol. Chem. 278 (2003) 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
  • 10
    • 0345097567 scopus 로고    scopus 로고
    • The Streptomyces coelicolor polynucleotide phosphorylase homologue, and not the putative poly(A) polymerase, can polyadenylate RNA
    • Sohlberg B., Huang J., and Cohen S.N. The Streptomyces coelicolor polynucleotide phosphorylase homologue, and not the putative poly(A) polymerase, can polyadenylate RNA. J. Bacteriol. 185 (2003) 7273-7278
    • (2003) J. Bacteriol. , vol.185 , pp. 7273-7278
    • Sohlberg, B.1    Huang, J.2    Cohen, S.N.3
  • 11
    • 30344450374 scopus 로고    scopus 로고
    • RNA polyadenylation in prokaryotes and organelles; different tails tell different tales
    • Slomovic S., Portnoy V., Liveanu V., and Schuster G. RNA polyadenylation in prokaryotes and organelles; different tails tell different tales. Crit. Rev. Plant Sci. 25 (2006) 65-77
    • (2006) Crit. Rev. Plant Sci. , vol.25 , pp. 65-77
    • Slomovic, S.1    Portnoy, V.2    Liveanu, V.3    Schuster, G.4
  • 13
    • 34250749349 scopus 로고    scopus 로고
    • Integration of chloroplast nucleic acid metabolism into the phosphate deprivation response in Chlamydomonas reinhardtii
    • Yehudai-Resheff S., Zimmer S.L., Komine Y., and Stern D.B. Integration of chloroplast nucleic acid metabolism into the phosphate deprivation response in Chlamydomonas reinhardtii. Plant Cell 19 (2007) 1023-1038
    • (2007) Plant Cell , vol.19 , pp. 1023-1038
    • Yehudai-Resheff, S.1    Zimmer, S.L.2    Komine, Y.3    Stern, D.B.4
  • 14
    • 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 D.C., Sarkar D., Su Z.Z., Holmes M., Valerie K., and Fisher P.B. 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. 99 (2002) 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
  • 16
    • 41549137572 scopus 로고    scopus 로고
    • S. Slomovic, G. Schuster, Stable PNPase RNAi silencing; its effect on the processing and adenylation of human mitochondrial RNA, RNA (in press).
    • S. Slomovic, G. Schuster, Stable PNPase RNAi silencing; its effect on the processing and adenylation of human mitochondrial RNA, RNA (in press).
  • 17
    • 41549163043 scopus 로고    scopus 로고
    • V. Portnoy, G. Palnizky, S. Yehudai-Resheff, F. Glaser, G. Schuster, Analysis of the human polynucleotide-phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts, RNA (in press).
    • V. Portnoy, G. Palnizky, S. Yehudai-Resheff, F. Glaser, G. Schuster, Analysis of the human polynucleotide-phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts, RNA (in press).
  • 18
    • 0030576503 scopus 로고    scopus 로고
    • Maturation pathways for E. coli tRNA precursors: a random multienzyme process in vivo
    • Li Z., and Deutscher M.P. Maturation pathways for E. coli tRNA precursors: a random multienzyme process in vivo. Cell 86 (1996) 503-512
    • (1996) Cell , vol.86 , pp. 503-512
    • Li, Z.1    Deutscher, M.P.2
  • 19
    • 0042858117 scopus 로고    scopus 로고
    • Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus
    • Ishii R., Nureki O., and Yokoyama S. Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus. J. Biol. Chem. 278 (2003) 32397-32404
    • (2003) J. Biol. Chem. , vol.278 , pp. 32397-32404
    • Ishii, R.1    Nureki, O.2    Yokoyama, S.3
  • 20
    • 0347683438 scopus 로고    scopus 로고
    • Probing the functional importance of the hexameric ring structure of RNase PH
    • Choi J.M., Park E.Y., Kim J.H., Chang S.K., and Cho Y. Probing the functional importance of the hexameric ring structure of RNase PH. J. Biol. Chem. 279 (2004) 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
  • 21
    • 34447119616 scopus 로고    scopus 로고
    • The exosome and RNA quality control in the nucleus
    • Vanacova S., and Stef R. The exosome and RNA quality control in the nucleus. EMBO Rep. 8 (2007) 651-657
    • (2007) EMBO Rep. , vol.8 , pp. 651-657
    • Vanacova, S.1    Stef, R.2
  • 23
    • 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 W.V., van Venrooij W.J., and Pruijn G.J. 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. 323 (2002) 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
  • 24
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
    • Symmons M.F., Jones G.H., and Luisi B.F. A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Structure 8 (2000) 1215-1226
    • (2000) Structure , vol.8 , pp. 1215-1226
    • Symmons, M.F.1    Jones, G.H.2    Luisi, B.F.3
  • 26
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: structural analysis and phylogenetic distribution
    • Zuo Y., and Deutscher M.P. Exoribonuclease superfamilies: structural analysis and phylogenetic distribution. Nucleic Acids Res. 29 (2001) 1017-1026
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2
  • 27
    • 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., and Schuster G. Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins. Plant Cell 15 (2003) 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
  • 30
    • 27644496002 scopus 로고    scopus 로고
    • Structural basis of 3′ end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core
    • Lorentzen E., and Conti E. Structural basis of 3′ end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core. Mol. Cell 20 (2005) 473-481
    • (2005) Mol. Cell , vol.20 , pp. 473-481
    • Lorentzen, E.1    Conti, E.2
  • 31
    • 33646523370 scopus 로고    scopus 로고
    • The exosome and the proteasome: nano-compartments for degradation
    • Lorentzen E., and Conti E. The exosome and the proteasome: nano-compartments for degradation. Cell 125 (2006) 651-654
    • (2006) Cell , vol.125 , pp. 651-654
    • Lorentzen, E.1    Conti, E.2
  • 32
    • 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., and Schuster G. RNA polyadenylation in Archaea: not observed in Haloferax while the exosome polyadenylates RNA in Sulfolobus. EMBO Rep. 6 (2005) 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
  • 33
    • 27644435644 scopus 로고    scopus 로고
    • Structural framework for the mechanism of archaeal exosomes in RNA processing
    • Buttner K., Wenig K., and Hopfner K.P. Structural framework for the mechanism of archaeal exosomes in RNA processing. Mol. Cell 20 (2005) 461-471
    • (2005) Mol. Cell , vol.20 , pp. 461-471
    • Buttner, K.1    Wenig, K.2    Hopfner, K.P.3
  • 34
    • 33748510412 scopus 로고    scopus 로고
    • The exosome: a macromolecular cage for controlled RNA degradation
    • Buttner K., Wenig K., and Hopfner K.P. The exosome: a macromolecular cage for controlled RNA degradation. Mol. Microbiol. 61 (2006) 1372-1379
    • (2006) Mol. Microbiol. , vol.61 , pp. 1372-1379
    • Buttner, K.1    Wenig, K.2    Hopfner, K.P.3
  • 35
    • 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., and Tollervey D. The exosome: a conserved eukaryotic RNA processing complex containing multiple 3′ to 5′ exoribonucleases. Cell 91 (1997) 457-466
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchel, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 36
    • 0032727868 scopus 로고    scopus 로고
    • The exosome: a proteasome for RNA?
    • van Hoof A., and Parker R. The exosome: a proteasome for RNA?. Cell 99 (1999) 347-350
    • (1999) Cell , vol.99 , pp. 347-350
    • van Hoof, A.1    Parker, R.2
  • 37
    • 4344573414 scopus 로고    scopus 로고
    • The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm
    • Raijmakers R., Schilders G., and Pruijn G.J. The exosome, a molecular machine for controlled RNA degradation in both nucleus and cytoplasm. Eur. J. Cell Biol. 83 (2004) 175-183
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 175-183
    • Raijmakers, R.1    Schilders, G.2    Pruijn, G.J.3
  • 39
    • 0036464532 scopus 로고    scopus 로고
    • Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3′ → 5′ exonuclease containing S1 and KH RNA-binding domains
    • Chekanova J.A., Dutko J.A., Mian I.S., and Belostotsky D.A. Arabidopsis thaliana exosome subunit AtRrp4p is a hydrolytic 3′ → 5′ exonuclease containing S1 and KH RNA-binding domains. Nucleic Acids Res. 30 (2002) 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
  • 40
    • 0035898660 scopus 로고    scopus 로고
    • The exosome of Trypanosoma brucei
    • Estevez A.M., Kempf T., and Clayton C. The exosome of Trypanosoma brucei. Embo J. 20 (2001) 3831-3839
    • (2001) Embo J. , vol.20 , pp. 3831-3839
    • Estevez, A.M.1    Kempf, T.2    Clayton, C.3
  • 41
    • 33845407784 scopus 로고    scopus 로고
    • Reconstitution, activities, and structure of the eukaryotic RNA exosome
    • Liu Q., Greimann J.C., and Lima C.D. Reconstitution, activities, and structure of the eukaryotic RNA exosome. Cell 127 (2006) 1223-1237
    • (2006) Cell , vol.127 , pp. 1223-1237
    • Liu, Q.1    Greimann, J.C.2    Lima, C.D.3
  • 42
    • 33846068920 scopus 로고    scopus 로고
    • A single subunit, Dis3, is essentially responsible for yeast exosome core activity
    • Dziembowski A., Lorentzen E., Conti E., and Seraphin B. A single subunit, Dis3, is essentially responsible for yeast exosome core activity. Nat. Struct. Mol. Biol. 14 (2007) 15-22
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 15-22
    • Dziembowski, A.1    Lorentzen, E.2    Conti, E.3    Seraphin, B.4
  • 43
    • 34447306927 scopus 로고    scopus 로고
    • The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines
    • Lin-Chao S., Chiou N.T., and Schuster G. The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines. J. Biomed. Sci. 14 (2007) 523-532
    • (2007) J. Biomed. Sci. , vol.14 , pp. 523-532
    • Lin-Chao, S.1    Chiou, N.T.2    Schuster, G.3
  • 44
    • 7044285063 scopus 로고    scopus 로고
    • The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli
    • Mohanty B.K., Maples V.F., and Kushner S.R. The Sm-like protein Hfq regulates polyadenylation dependent mRNA decay in Escherichia coli. Mol. Microbiol. 54 (2004) 905-920
    • (2004) Mol. Microbiol. , vol.54 , pp. 905-920
    • Mohanty, B.K.1    Maples, V.F.2    Kushner, S.R.3
  • 45
    • 12544256747 scopus 로고    scopus 로고
    • Stimulation of poly(A) synthesis by Escherichia coli poly(A)polymerase I is correlated with Hfq binding to poly(A) tails
    • Folichon M., Allemand F., Regnier P., and Hajnsdorf E. Stimulation of poly(A) synthesis by Escherichia coli poly(A)polymerase I is correlated with Hfq binding to poly(A) tails. FEBS J. 272 (2005) 454-463
    • (2005) FEBS J. , vol.272 , pp. 454-463
    • Folichon, M.1    Allemand, F.2    Regnier, P.3    Hajnsdorf, E.4
  • 46
    • 12344330602 scopus 로고    scopus 로고
    • An important role for RNase R in mRNA decay
    • Cheng Z.F., and Deutscher M.P. An important role for RNase R in mRNA decay. Mol. Cell 17 (2005) 313-318
    • (2005) Mol. Cell , vol.17 , pp. 313-318
    • Cheng, Z.F.1    Deutscher, M.P.2
  • 47
    • 0029828944 scopus 로고    scopus 로고
    • Addition of poly(A)-rich sequences to endonucleolytic cleavage sites in the degradation of spinach chloroplast mRNA
    • Lisitsky I., Klaff P., and Schuster G. Addition of poly(A)-rich sequences to endonucleolytic cleavage sites in the degradation of spinach chloroplast mRNA. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 13398-13403
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 13398-13403
    • Lisitsky, I.1    Klaff, P.2    Schuster, G.3
  • 48
    • 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 G.H., Bechhofer D.H., and Olmedo-Alvarez G. Addition of poly(A) and heteropolymeric 3′ ends in Bacillus subtilis wild-type and polynucleotide phosphorylase-deficient strains. J. Bacteriol. 187 (2005) 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
  • 49
    • 33845606715 scopus 로고    scopus 로고
    • RNA polyadenylation and degradation in different archaea; roles of the exosome and RNase R
    • Portnoy V., and Schuster G. RNA polyadenylation and degradation in different archaea; roles of the exosome and RNase R. Nucleic Acids Res. 34 (2006) 5923-5931
    • (2006) Nucleic Acids Res. , vol.34 , pp. 5923-5931
    • Portnoy, V.1    Schuster, G.2
  • 50
    • 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., and Stepien P.P. The yeast mitochondrial degradosome. Its composition, interplay between RNA helicase and RNase activities and the role in mitochondrial RNA metabolism. J. Biol. Chem. 278 (2003) 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
  • 52
    • 17844366081 scopus 로고    scopus 로고
    • Transcription and RNA-processing in fission yeast mitochondria
    • Schafer B., Hansen M., and Lang B.F. Transcription and RNA-processing in fission yeast mitochondria. RNA 11 (2005) 785-795
    • (2005) RNA , vol.11 , pp. 785-795
    • Schafer, B.1    Hansen, M.2    Lang, B.F.3
  • 53
    • 14044264228 scopus 로고    scopus 로고
    • Opposing effects of polyadenylation on the stability of edited and unedited mitochondrial RNAs in Trypanosoma brucei
    • Kao C.Y., and Read L.K. Opposing effects of polyadenylation on the stability of edited and unedited mitochondrial RNAs in Trypanosoma brucei. Mol. Cell. Biol. 25 (2005) 1634-1644
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1634-1644
    • Kao, C.Y.1    Read, L.K.2
  • 55
    • 31544440417 scopus 로고    scopus 로고
    • Adenylation and exosome-mediated degradation of cotranscriptionally cleaved pre-messenger RNA in human cells
    • West S., Gromak N., Norbury C.J., and Proudfoot N.J. Adenylation and exosome-mediated degradation of cotranscriptionally cleaved pre-messenger RNA in human cells. Mol. Cell 21 (2006) 437-443
    • (2006) Mol. Cell , vol.21 , pp. 437-443
    • West, S.1    Gromak, N.2    Norbury, C.J.3    Proudfoot, N.J.4
  • 56
    • 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 R.N., Glavin J.D., Chen H.W., French S.W., Teitell M.A., and Koehler C.M. A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space. Mol. Cell. Biol. 26 (2006) 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
  • 57
    • 34249026025 scopus 로고    scopus 로고
    • A family of poly(U) polymerases
    • Kwak J.E., and Wickens M. A family of poly(U) polymerases. RNA 13 (2007) 860-867
    • (2007) RNA , vol.13 , pp. 860-867
    • Kwak, J.E.1    Wickens, M.2
  • 58
    • 34248225381 scopus 로고    scopus 로고
    • Efficient RNA polyuridylation by noncanonical poly(A) polymerases
    • Rissland O.S., Mikulasova A., and Norbury C.J. Efficient RNA polyuridylation by noncanonical poly(A) polymerases. Mol. Cell. Biol. 27 (2007) 3612-3624
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3612-3624
    • Rissland, O.S.1    Mikulasova, A.2    Norbury, C.J.3
  • 59
    • 33751297741 scopus 로고    scopus 로고
    • The Cid1 family of non-canonical poly(A) polymerases
    • Stevenson A.L., and Norbury C.J. The Cid1 family of non-canonical poly(A) polymerases. Yeast 23 (2006) 991-1000
    • (2006) Yeast , vol.23 , pp. 991-1000
    • Stevenson, A.L.1    Norbury, C.J.2
  • 60
    • 19644400971 scopus 로고    scopus 로고
    • Uridine addition after microRNA-directed cleavage
    • Shen B., and Goodman H.M. Uridine addition after microRNA-directed cleavage. Science 306 (2004) 997
    • (2004) Science , vol.306 , pp. 997
    • Shen, B.1    Goodman, H.M.2
  • 61
    • 2442665253 scopus 로고    scopus 로고
    • Sequence motifs that distinguish ATP(CTP): tRNA nucleotidyl transferases from eubacterial poly(A) polymerases
    • Martin G., and Keller W. Sequence motifs that distinguish ATP(CTP): tRNA nucleotidyl transferases from eubacterial poly(A) polymerases. RNA 10 (2004) 899-906
    • (2004) RNA , vol.10 , pp. 899-906
    • Martin, G.1    Keller, W.2
  • 62
    • 4143073655 scopus 로고    scopus 로고
    • Exchange of regions between bacterial poly(A) polymerase and the CCA-adding enzyme generates altered specificities
    • Betat H., Rammelt C., Martin G., and Morl M. Exchange of regions between bacterial poly(A) polymerase and the CCA-adding enzyme generates altered specificities. Mol. Cell 15 (2004) 389-398
    • (2004) Mol. Cell , vol.15 , pp. 389-398
    • Betat, H.1    Rammelt, C.2    Martin, G.3    Morl, M.4
  • 63
    • 33645214213 scopus 로고    scopus 로고
    • Mutation pressure and the evolution of organelle genomic architecture
    • Lynch M., Koskella B., and Schaack S. Mutation pressure and the evolution of organelle genomic architecture. Science 311 (2006) 1727-1730
    • (2006) Science , vol.311 , pp. 1727-1730
    • Lynch, M.1    Koskella, B.2    Schaack, S.3
  • 64
    • 0019444843 scopus 로고
    • tRNA punctuation model of RNA processing in human mitochondria
    • Ojala D., Montoya J., and Attardi G. tRNA punctuation model of RNA processing in human mitochondria. Nature 290 (1981) 470-474
    • (1981) Nature , vol.290 , pp. 470-474
    • Ojala, D.1    Montoya, J.2    Attardi, G.3
  • 65
    • 0036267108 scopus 로고    scopus 로고
    • cDNA cloning confirms the polyadenylation of RNA decay intermediates in Streptomyces coelicolor
    • Bralley P., and Jones G.H. cDNA cloning confirms the polyadenylation of RNA decay intermediates in Streptomyces coelicolor. Microbiology 148 (2002) 1421-1425
    • (2002) Microbiology , vol.148 , pp. 1421-1425
    • Bralley, P.1    Jones, G.H.2
  • 66
    • 0034072252 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase, RNase II and RNase E play different roles in the in vivo modulation of polyadenylation in Escherichia coli
    • Mohanty B.K., and Kushner S.R. Polynucleotide phosphorylase, RNase II and RNase E play different roles in the in vivo modulation of polyadenylation in Escherichia coli. Mol. Microbiol. 36 (2000) 982-994
    • (2000) Mol. Microbiol. , vol.36 , pp. 982-994
    • Mohanty, B.K.1    Kushner, S.R.2
  • 68
    • 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., and Ueda T. Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase. J. Biol. Chem. 280 (2005) 19721-31927
    • (2005) J. Biol. Chem. , vol.280 , pp. 19721-31927
    • Nagaike, T.1    Suzuki, T.2    Katoh, T.3    Ueda, T.4
  • 69
    • 33645739358 scopus 로고    scopus 로고
    • Yeast Trf5p is a nuclear poly(A) polymerase
    • Houseley J., and Tollervey D. Yeast Trf5p is a nuclear poly(A) polymerase. EMBO Rep. 7 (2006) 205-211
    • (2006) EMBO Rep. , vol.7 , pp. 205-211
    • Houseley, J.1    Tollervey, D.2
  • 70
    • 27644539312 scopus 로고    scopus 로고
    • Trf4 and Trf5 proteins of Saccharomyces cerevisiae exhibit poly(A) RNA polymerase activity but no DNA polymerase activity
    • Haracska L., Johnson R.E., Prakash L., and Prakash S. Trf4 and Trf5 proteins of Saccharomyces cerevisiae exhibit poly(A) RNA polymerase activity but no DNA polymerase activity. Mol. Cell. Biol. 25 (2005) 10183-10189
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10183-10189
    • Haracska, L.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4
  • 71
    • 29844458585 scopus 로고    scopus 로고
    • Contributions of Trf4p- and Trf5p-dependent polyadenylation to the processing and degradative functions of the yeast nuclear exosome
    • Egecioglu D.E., Henras A.K., and Chanfreau G.F. Contributions of Trf4p- and Trf5p-dependent polyadenylation to the processing and degradative functions of the yeast nuclear exosome. RNA 12 (2006) 26-32
    • (2006) RNA , vol.12 , pp. 26-32
    • Egecioglu, D.E.1    Henras, A.K.2    Chanfreau, G.F.3
  • 72
    • 0037136552 scopus 로고    scopus 로고
    • A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans
    • Wang L., Eckmann C.R., Kadyk L.C., Wickens M., and Kimble J. A regulatory cytoplasmic poly(A) polymerase in Caenorhabditis elegans. Nature 419 (2002) 312-316
    • (2002) Nature , vol.419 , pp. 312-316
    • Wang, L.1    Eckmann, C.R.2    Kadyk, L.C.3    Wickens, M.4    Kimble, J.5
  • 74
    • 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. 71 (2002) 285-389
    • (2002) Prog. Nucleic Acid Res. Mol. Biol. , vol.71 , pp. 285-389
    • Edmonds, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.