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Volumn 67, Issue 3, 2011, Pages 381-394

Mutational analysis of Arabidopsis chloroplast polynucleotide phosphorylase reveals roles for both RNase PH core domains in polyadenylation, RNA 3′-end maturation and intron degradation

Author keywords

chloroplast; intron; polynucleotide phosphorylase; ribonuclease; RNA; splicing

Indexed keywords

ARABIDOPSIS; CATALYTIC SITES; CHLOROPLAST; IN-VITRO; IN-VITRO ANALYSIS; IN-VIVO; INTRON; MUTATIONAL ANALYSIS; PHOSPHOROLYSIS; PLANT ORGANELLES; POLYADENYLATION; POLYNUCLEOTIDE PHOSPHORYLASE; RECOMBINANT ENZYMES; RIBONUCLEASE; TWO-LINE; WILD-TYPE PLANTS;

EID: 80955177475     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/j.1365-313X.2011.04601.x     Document Type: Article
Times cited : (39)

References (50)
  • 1
    • 33845674625 scopus 로고    scopus 로고
    • Arabidopsis orthologs of maize chloroplast splicing factors promote splicing of orthologous and species-specific group II introns
    • DOI 10.1104/pp.106.088096
    • Asakura, Y., and, Barkan, A., (2006) Arabidopsis orthologs of maize chloroplast splicing factors promote splicing of orthologous and species-specific group II introns. Plant Physiol. 142, 1656-1663. (Pubitemid 44956940)
    • (2006) Plant Physiology , vol.142 , Issue.4 , pp. 1656-1663
    • Asakura, Y.1    Barkan, A.2
  • 3
    • 0024639674 scopus 로고
    • Tissue-dependent plastid RNA splicing in maize: Transcripts from four plastid genes are predominantly unspliced in leaf meristems and roots
    • Barkan, A., (1989) Tissue-dependent plastid RNA splicing in maize: transcripts from four plastid genes are predominantly unspliced in leaf meristems and roots. Plant Cell, 1, 437-446.
    • (1989) Plant Cell , vol.1 , pp. 437-446
    • Barkan, A.1
  • 4
    • 0001355547 scopus 로고
    • Plastid transcription activity and DNA copy number increase early in barley chloroplast development
    • Baumgartner, B.J., Rapp, J.C., and, Mullet, J.E., (1989) Plastid transcription activity and DNA copy number increase early in barley chloroplast development. Plant Physiol. 89, 1011-1018.
    • (1989) Plant Physiol. , vol.89 , pp. 1011-1018
    • Baumgartner, B.J.1    Rapp, J.C.2    Mullet, J.E.3
  • 5
    • 18744378589 scopus 로고    scopus 로고
    • RNR1, a 3′-5′ exoribonuclease belonging to the RNR superfamily, catalyzes 3′ maturation of chloroplast ribosomal RNAs in Arabidopsis thaliana
    • DOI 10.1093/nar/gki576
    • Bollenbach, T.J., Lange, H., Gutierrez, R., Erhardt, M., Stern, D.B., and, Gagliardi, D., (2005) RNR1, a 3′-5′ exoribonuclease belonging to the RNR superfamily, catalyzes 3′ maturation of chloroplast ribosomal RNAs in Arabidopsis thaliana. Nucleic Acids Res. 33, 2751-2763. (Pubitemid 41511293)
    • (2005) Nucleic Acids Research , vol.33 , Issue.8 , pp. 2751-2763
    • Bollenbach, T.J.1    Lange, H.2    Gutierrez, R.3    Erhardt, M.4    Stern, D.B.5    Gagliardi, D.6
  • 6
    • 38949108938 scopus 로고    scopus 로고
    • Degradation of plastid unspliced transcripts and lariat group II introns
    • DOI 10.1016/j.biochi.2007.10.006, PII S0300908407003008
    • del Campo, E.M., and, Casano, L.M., (2008) Degradation of plastid unspliced transcripts and lariat group II introns. Biochimie, 90, 474-483. (Pubitemid 351232120)
    • (2008) Biochimie , vol.90 , Issue.3 , pp. 474-483
    • Del Campo, E.M.1    Casano, L.M.2
  • 8
    • 0027220698 scopus 로고
    • Promiscuous exoribonucleases of Escherichia coli
    • Deutscher, M.P., (1993) Promiscuous exoribonucleases of Escherichia coli. J. Bacteriol. 175, 4577-4583. (Pubitemid 23220238)
    • (1993) Journal of Bacteriology , vol.175 , Issue.15 , pp. 4577-4583
    • Deutscher, M.P.1
  • 9
    • 77956533718 scopus 로고    scopus 로고
    • (p)ppGpp Inhibits polynucleotide phosphorylase from Streptomyces but not from Escherichia coli and increases the stability of bulk mRNA in Streptomyces coelicolor
    • Gatewood, M.L., and, Jones, G.H., (2010) (p)ppGpp Inhibits polynucleotide phosphorylase from Streptomyces but not from Escherichia coli and increases the stability of bulk mRNA in Streptomyces coelicolor. J. Bacteriol. 192, 4275-4280.
    • (2010) J. Bacteriol. , vol.192 , pp. 4275-4280
    • Gatewood, M.L.1    Jones, G.H.2
  • 10
    • 0001719080 scopus 로고
    • Enzymatic synthesis and breakdown of polynucleotides; Polynucleotide phosphorylase
    • Grunberg-Manago, M., and, Ochoa, S., (1955) Enzymatic synthesis and breakdown of polynucleotides; polynucleotide phosphorylase. J. Am. Chem. Soc. 77, 3165-3166.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 3165-3166
    • Grunberg-Manago, M.1    Ochoa, S.2
  • 11
    • 0029917715 scopus 로고    scopus 로고
    • Chloroplast mRNA 3′-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins
    • Hayes, R., Kudla, J., Schuster, G., Gabay, L., Maliga, P., and, Gruissem, W., (1996) Chloroplast mRNA 3′-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA binding proteins. EMBO J. 15, 1132-1141.
    • (1996) EMBO J. , vol.15 , pp. 1132-1141
    • Hayes, R.1    Kudla, J.2    Schuster, G.3    Gabay, L.4    Maliga, P.5    Gruissem, W.6
  • 12
    • 33645233480 scopus 로고    scopus 로고
    • Relaxed transcription in Arabidopsis mitochondria is counterbalanced by RNA stability control mediated by polyadenylation and polynucleotide phosphorylase
    • Holec, S., Lange, H., Kuhn, K., Alioua, M., Borner, T., and, Gagliardi, D., (2006) Relaxed transcription in Arabidopsis mitochondria is counterbalanced by RNA stability control mediated by polyadenylation and polynucleotide phosphorylase. Mol. Cell. Biol. 26, 2869-2876.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2869-2876
    • Holec, S.1    Lange, H.2    Kuhn, K.3    Alioua, M.4    Borner, T.5    Gagliardi, D.6
  • 13
    • 0036382938 scopus 로고    scopus 로고
    • Mutational analysis of polynucleotide phosphorylase from Escherichia coli
    • Jarrige, A., Brechemier-Baey, D., Mathy, N., Duche, O., and, Portier, C., (2002) Mutational analysis of polynucleotide phosphorylase from Escherichia coli. J. Mol. Biol. 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
  • 14
    • 0031106356 scopus 로고    scopus 로고
    • Nuclear mutations that block group II RNA splicing in maize chloroplasts reveal several intron classes with distinct requirements for splicing factors
    • DOI 10.1105/tpc.9.3.283
    • Jenkins, B.D., Kulhanek, D.J., and, Barkan, A., (1997) Nuclear mutations that block group II RNA splicing in maize chloroplasts reveal several intron classes with distinct requirements for splicing factors. Plant Cell, 9, 283-296. (Pubitemid 27176819)
    • (1997) Plant Cell , vol.9 , Issue.3 , pp. 283-296
    • Jenkins, B.D.1    Kulhanek, D.J.2    Barkan, A.3
  • 15
    • 0033993926 scopus 로고    scopus 로고
    • Polyadenylation of three classes of chloroplast RNA in Chlamydomonas reinhardtii
    • DOI 10.1017/S1355838200992252
    • Komine, Y., Kwong, L., Anguera, M.C., Schuster, G., and, Stern, D.B., (2000) Polyadenylation of three classes of chloroplast RNA in Chlamydomonas reinhardtii. RNA, 6, 598-607. (Pubitemid 30212237)
    • (2000) RNA , vol.6 , Issue.4 , pp. 598-607
    • Komine, Y.1    Kwong, L.2    Anguera, M.C.3    Schuster, G.4    Stern, D.B.5
  • 16
    • 0033048415 scopus 로고    scopus 로고
    • The C-terminal half of RNase E, which organizes the Escherichia coli degradosome, participates in mRNA degradation but not rRNA processing in vivo
    • DOI 10.1046/j.1365-2958.1999.01465.x
    • Lopez, P.J., Marchand, I., Joyce, S.A., and, Dreyfus, M., (1999) The C-terminal half of RNase E, which organizes the Escherichia coli degradosome, participates in mRNA degradation but not rRNA processing in vivo. Mol. Microbiol. 33, 188-199. (Pubitemid 29304199)
    • (1999) Molecular Microbiology , vol.33 , Issue.1 , pp. 188-199
    • Lopez, P.J.1    Marchand, I.2    Joyce, S.A.3    Dreyfus, M.4
  • 18
    • 70349648633 scopus 로고    scopus 로고
    • Abnormal physiological and molecular mutant phenotypes link chloroplast polynucleotide phosphorylase to the phosphorus deprivation response in Arabidopsis
    • Marchive, C., Yehudai-Resheff, S., Germain, A., Fei, Z., Jiang, X., Judkins, J., Wu, H., Fernie, A.R., Fait, A., and, Stern, D.B., (2009) Abnormal physiological and molecular mutant phenotypes link chloroplast polynucleotide phosphorylase to the phosphorus deprivation response in Arabidopsis. Plant Physiol. 151, 905-924.
    • (2009) Plant Physiol. , vol.151 , pp. 905-924
    • Marchive, C.1    Yehudai-Resheff, S.2    Germain, A.3    Fei, Z.4    Jiang, X.5    Judkins, J.6    Wu, H.7    Fernie, A.R.8    Fait, A.9    Stern, D.B.10
  • 19
    • 0024428420 scopus 로고
    • Comparative and functional anatomy of group II catalytic introns - A review
    • DOI 10.1016/0378-1119(89)90026-7
    • Michel, F., Umesono, K., and, Ozeki, H., (1989) Comparative and functional anaotmy of group II catalytic introns - a review. Gene, 82, 5-30. (Pubitemid 19248654)
    • (1989) Gene , vol.82 , Issue.1 , pp. 5-30
    • Michel, F.1    Umesono, K.2    Ozeki, H.3
  • 20
    • 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., (2000) Polynucleotide phosphorylase functions both as a 3′ to 5′ exonuclease and a poly(A) polymerase in Escherichia coli. Proc. Natl Acad. Sci. USA, 97, 11966-11971.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 11966-11971
    • Mohanty, B.K.1    Kushner, S.R.2
  • 21
    • 0036890406 scopus 로고    scopus 로고
    • Web-based primer design for single nucleotide polymorphism analysis
    • DOI 10.1016/S0168-9525(02)02820-2, PII S0168952502028202
    • Neff, M.M., Turk, E., and, Kalishman, M., (2002) Web-based primer design for single nucleotide polymorphism analysis. Trends Genet. 18, 613-615. (Pubitemid 35346679)
    • (2002) Trends in Genetics , vol.18 , Issue.12 , pp. 613-615
    • Neff, M.M.1    Turk, E.2    Kalishman, M.3
  • 22
    • 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, A.J., and, Luisi, B.F., (2009) 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. 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
  • 24
    • 4944238979 scopus 로고    scopus 로고
    • AtmtPNPase is required for multiple aspects of the 18S rRNA metabolism in Arabidopsis thaliana mitochondria
    • DOI 10.1093/nar/gkh852
    • Perrin, R., Lange, H., Grienenberger, J.M., and, Gagliardi, D., (2004a) AtmtPNPase is required for multiple aspects of the 18S rRNA metabolism in Arabidopsis thaliana mitochondria. Nucleic Acids Res. 32, 5174-5182. (Pubitemid 39445504)
    • (2004) Nucleic Acids Research , vol.32 , Issue.17 , pp. 5174-5182
    • Perrin, R.1    Lange, H.2    Grienenberger, J.-M.3    Gagliardi, D.4
  • 26
    • 67651171227 scopus 로고    scopus 로고
    • Site-specific binding of a PPR protein defines and stabilizes 5′ and 3′ mRNA termini in chloroplasts
    • Pfalz, J., Bayraktar, O.A., Prikryl, J., and, Barkan, A., (2009) Site-specific binding of a PPR protein defines and stabilizes 5′ and 3′ mRNA termini in chloroplasts. EMBO J. 28, 2042-2052.
    • (2009) EMBO J. , vol.28 , pp. 2042-2052
    • Pfalz, J.1    Bayraktar, O.A.2    Prikryl, J.3    Barkan, A.4
  • 27
    • 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
    • DOI 10.1261/rna.698108
    • Portnoy, V., Palnizky, G., Yehudai-Resheff, S., Glaser, F., and, Schuster, G., (2008) Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts. RNA, 14, 297-309. (Pubitemid 351171590)
    • (2008) RNA , vol.14 , Issue.2 , pp. 297-309
    • Portnoy, V.1    Palnizky, G.2    Yehudai-Resheff, S.3    Glaser, F.4    Schuster, G.5
  • 29
    • 64049109732 scopus 로고    scopus 로고
    • RNA polyadenylation and decay in mitochondria and chloroplasts
    • Schuster, G., and, Stern, D., (2009) RNA polyadenylation and decay in mitochondria and chloroplasts. Prog. Mol. Biol. Transl. Sci. 85, 393-422.
    • (2009) Prog. Mol. Biol. Transl. Sci. , vol.85 , pp. 393-422
    • Schuster, G.1    Stern, D.2
  • 30
    • 33751536092 scopus 로고    scopus 로고
    • A promoter switch that can rescue a plant sigma factor mutant
    • DOI 10.1016/j.febslet.2006.11.010, PII S0014579306013263
    • Schweer, J., Loschelder, H., and, Link, G., (2006) A promoter switch that can rescue a plant sigma factor mutant. FEBS Lett. 580, 6617-6622. (Pubitemid 44834394)
    • (2006) FEBS Letters , vol.580 , Issue.28-29 , pp. 6617-6622
    • Schweer, J.1    Loschelder, H.2    Link, G.3
  • 31
    • 55549093442 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli PNPase: Central channel residues are involved in processive RNA degradation
    • Shi, Z., Yang, W.Z., Lin-Chao, S., Chak, K.F., and, Yuan, H.S., (2008) Crystal structure of Escherichia coli PNPase: central channel residues are involved in processive RNA degradation. RNA, 14, 2361-2371.
    • (2008) RNA , vol.14 , pp. 2361-2371
    • Shi, Z.1    Yang, W.Z.2    Lin-Chao, S.3    Chak, K.F.4    Yuan, H.S.5
  • 32
    • 38649115643 scopus 로고    scopus 로고
    • Stable PNPase RNAi silencing: Its effect on the processing and adenylation of human mitochondrial RNA
    • DOI 10.1261/rna.697308
    • Slomovic, S., and, Schuster, G., (2008) Stable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNA. RNA, 14, 310-323. (Pubitemid 351171591)
    • (2008) RNA , vol.14 , Issue.2 , pp. 310-323
    • Slomovic, S.1    Schuster, G.2
  • 33
    • 58249092049 scopus 로고    scopus 로고
    • Detection and characterization of polyadenylated RNA in Eukarya, Bacteria, Archaea, and organelles
    • Slomovic, S., Portnoy, V., and, Schuster, G., (2008a) Detection and characterization of polyadenylated RNA in Eukarya, Bacteria, Archaea, and organelles. Methods Enzymol. 447, 501-520.
    • (2008) Methods Enzymol. , vol.447 , pp. 501-520
    • Slomovic, S.1    Portnoy, V.2    Schuster, G.3
  • 35
    • 0033996954 scopus 로고    scopus 로고
    • Action of RNase II and polynucleotide phosphorylase against RNAs containing stem-loops of defined structure
    • DOI 10.1128/JB.182.9.2422-2427.2000
    • Spickler, C., and, Mackie, G.A., (2000) Action of RNase II and polynucleotide phosphorylase against RNAs containing stem-loops of defined structure. J. Bacteriol. 182, 2422-2427. (Pubitemid 30212898)
    • (2000) Journal of Bacteriology , vol.182 , Issue.9 , pp. 2422-2427
    • Spickler, C.1    Mackie, G.A.2
  • 36
    • 0023663880 scopus 로고
    • Control of plastid gene expression: 3′ inverted repeats act as mRNA processing and stabilizing elements, but do not terminate transcription
    • Stern, D.B., and, Gruissem, W., (1987) Control of plastid gene expression: 3′ inverted repeats act as mRNA processing and stabilizing elements, but do not terminate transcription. Cell, 51, 1145-1157.
    • (1987) Cell , vol.51 , pp. 1145-1157
    • Stern, D.B.1    Gruissem, W.2
  • 38
    • 0034435974 scopus 로고    scopus 로고
    • A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation
    • DOI 10.1016/S0969-2126(00)00521-9, PII S0969212600005219
    • Symmons, M.F., Jones, G.H., and, Luisi, B.F., (2000) A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Structure Fold Des. 8, 1215-1226. (Pubitemid 32667486)
    • (2000) Structure , vol.8 , Issue.11 , pp. 1215-1226
    • Symmons, M.F.1    Jones, G.H.2    Luisi, B.F.3
  • 39
    • 0036164937 scopus 로고    scopus 로고
    • Running rings around RNA: A superfamily of phosphate-dependent RNases
    • DOI 10.1016/S0968-0004(01)01999-5, PII S0968000401019995
    • Symmons, M.F., Williams, M.G., Luisi, B.F., Jones, G.H., and, Carpousis, A.J., (2002) Running rings around RNA: a superfamily of phosphate-dependent RNases. Trends Biochem. Sci. 27, 11-18. (Pubitemid 34131620)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.1 , pp. 11-18
    • Symmons, M.F.1    Williams, M.G.2    Luisi, B.F.3    Jones, G.H.4    Carpousis, A.J.5
  • 41
    • 0037099679 scopus 로고    scopus 로고
    • Lariat formation and a hydrolytic pathway in plant chloroplast group II intron splicing
    • DOI 10.1093/emboj/cdf359
    • Vogel, J., and, Borner, T., (2002) Lariat formation and a hydrolytic pathway in plant chloroplast group II intron splicing. EMBO J. 21, 3794-3803. (Pubitemid 34787052)
    • (2002) EMBO Journal , vol.21 , Issue.14 , pp. 3794-3803
    • Vogel, J.1    Borner, T.2
  • 42
    • 0037121925 scopus 로고    scopus 로고
    • PNPase activity determines the efficiency of mRNA 3′-end processing, the degradation of tRNA and the extent of polyadenylation in chloroplasts
    • DOI 10.1093/emboj/cdf686
    • Walter, M., Kilian, J., and, Kudla, J., (2002) PNPase activity determines the efficiency of mRNA 3′-end processing, the degradation of tRNA and the extent of polyadenylation in chloroplasts. EMBO J. 21, 6905-6914. (Pubitemid 36014562)
    • (2002) EMBO Journal , vol.21 , Issue.24 , pp. 6905-6914
    • Walter, M.1    Kilian, J.2    Kudla, J.3
  • 44
    • 77955320529 scopus 로고    scopus 로고
    • PNPase regulates RNA import into mitochondria
    • Wang, G., Chen, H.W., Oktay, Y., et al. (2010) PNPase regulates RNA import into mitochondria. Cell, 142, 456-467.
    • (2010) Cell , vol.142 , pp. 456-467
    • Wang, G.1    Chen, H.W.2    Oktay, Y.3
  • 45
    • 39049185411 scopus 로고    scopus 로고
    • Isolation of chloroplast proteins from Arabidopsis thaliana for proteome analysis
    • van Wijk, K.J., Peltier, J.B., and, Giacomelli, L., (2007) Isolation of chloroplast proteins from Arabidopsis thaliana for proteome analysis. Methods Mol. Biol. 355, 43-48.
    • (2007) Methods Mol. Biol. , vol.355 , pp. 43-48
    • Van Wijk, K.J.1    Peltier, J.B.2    Giacomelli, L.3
  • 46
    • 0034934778 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts
    • DOI 10.1128/MCB.21.16.5408-5416.2001
    • Yehudai-Resheff, S., Hirsh, M., and, Schuster, G., (2001) Polynucleotide phosphorylase functions as both an exonuclease and a poly(A) polymerase in spinach chloroplasts. Mol. Cell. Biol. 21, 5408-5416. (Pubitemid 32702445)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.16 , pp. 5408-5416
    • Yehudai-Resheff, S.1    Hirsh, M.2    Schuster, G.3
  • 47
    • 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
    • DOI 10.1105/tpc.013326
    • Yehudai-Resheff, S., Portnoy, V., Yogev, S., Adir, N., and, Schuster, G., (2003) Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins. Plant Cell, 15, 2003-2019. (Pubitemid 37144057)
    • (2003) Plant Cell , vol.15 , Issue.9 , pp. 2003-2019
    • Yehudai-Resheff, S.1    Portnoy, V.2    Yogev, S.3    Adir, N.4    Schuster, G.5
  • 48
    • 34250749349 scopus 로고    scopus 로고
    • Integration of chloroplast nucleic acid metabolism into the phosphate deprivation response in Chlamydomonas reinhardtii
    • DOI 10.1105/tpc.106.045427
    • Yehudai-Resheff, S., Zimmer, S.L., Komine, Y., and, Stern, D.B., (2007) Integration of chloroplast nucleic acid metabolism into the phosphate deprivation response in Chlamydomonas reinhardtii. Plant Cell, 19, 1023-1038. (Pubitemid 46953244)
    • (2007) Plant Cell , vol.19 , Issue.3 , pp. 1023-1038
    • Yehudai-Resheff, S.1    Zimmer, S.L.2    Komine, Y.3    Stern, D.B.4
  • 49
    • 33846907792 scopus 로고    scopus 로고
    • Nucleus-encoded plastid sigma factor SIG3 transcribes specifically the psbN gene in plastids
    • DOI 10.1093/nar/gkl1067
    • Zghidi, W., Merendino, L., Cottet, A., Mache, R., and, Lerbs-Mache, S., (2007) Nucleus-encoded plastid sigma factor SIG3 transcribes specifically the psbN gene in plastids. Nucleic Acids Res. 35, 455-464. (Pubitemid 46232063)
    • (2007) Nucleic Acids Research , vol.35 , Issue.2 , pp. 455-464
    • Zghidi, W.1    Merendino, L.2    Cottet, A.3    Mache, R.4    Lerbs-Mache, S.5
  • 50
    • 67649476386 scopus 로고    scopus 로고
    • Polyadenylation in Arabidopsis and Chlamydomonas organelles: The input of nucleotidyltransferases, poly(A) polymerases and polynucleotide phosphorylase
    • Zimmer, S.L., Schein, A., Zipor, G., Stern, D.B., and, Schuster, G., (2009) Polyadenylation in Arabidopsis and Chlamydomonas organelles: the input of nucleotidyltransferases, poly(A) polymerases and polynucleotide phosphorylase. Plant J. 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


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