메뉴 건너뛰기




Volumn 126, Issue 1, 2015, Pages 171-183

Genetic and genomic analysis of RNases in model cyanobacteria

Author keywords

Biofuels; Comparative genomics; Cyanobacteria; mRNA; Photosynthesis; Ribonuclease; RNA; Synthetic biology

Indexed keywords

BACTERIAL PROTEIN; MESSENGER RNA; RIBONUCLEASE; RIBONUCLEASE III;

EID: 84942839163     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-015-0076-2     Document Type: Article
Times cited : (22)

References (51)
  • 1
    • 72949089708 scopus 로고    scopus 로고
    • Global signatures of protein and mRNA expression levels
    • 4089977 1:CAS:528:DC%2BD1MXhtl2ks7fK
    • Abreu RD, Penalva LO, Marcotte EM, Vogel C (2009) Global signatures of protein and mRNA expression levels. Mol BioSyst 5(12):1512-1526
    • (2009) Mol BioSyst , vol.5 , Issue.12 , pp. 1512-1526
    • Abreu, R.D.1    Penalva, L.O.2    Marcotte, E.M.3    Vogel, C.4
  • 2
    • 77954952126 scopus 로고    scopus 로고
    • Messenger RNA turnover processes in Escherichia coli, Bacillus subtilis, and emerging studies in Staphylococcus aureus
    • 2777011 19936110
    • Anderson KL, Dunman PM (2009) Messenger RNA turnover processes in Escherichia coli, Bacillus subtilis, and emerging studies in Staphylococcus aureus. Int J Microbiol 2009:525491
    • (2009) Int J Microbiol , vol.2009 , pp. 525491
    • Anderson, K.L.1    Dunman, P.M.2
  • 3
    • 83355169557 scopus 로고    scopus 로고
    • Two pathways for RNase e action in Escherichia coli in vivo and bypass of its essentiality in mutants defective for Rho-dependent transcription termination
    • 1:CAS:528:DC%2BC38XhtFSgsQ%3D%3D 22026368
    • Anupama K, Leela JK, Gowrishankar J (2011) Two pathways for RNase E action in Escherichia coli in vivo and bypass of its essentiality in mutants defective for Rho-dependent transcription termination. Mol Microbiol 82(6):1330-1348
    • (2011) Mol Microbiol , vol.82 , Issue.6 , pp. 1330-1348
    • Anupama, K.1    Leela, J.K.2    Gowrishankar, J.3
  • 4
    • 0015883541 scopus 로고
    • Degradation of RNA in Escherichia coli. A hypothesis
    • 1:CAS:528:DyaE3sXkvV2ns7k%3D 4577538
    • Apirion D (1973) Degradation of RNA in Escherichia coli. A hypothesis. Mol Gen Genet 122(4):313-322
    • (1973) Mol Gen Genet , vol.122 , Issue.4 , pp. 313-322
    • Apirion, D.1
  • 5
    • 0016676008 scopus 로고
    • Mapping and characterization of a mutation in Escherichia coli that reduces the level of ribonuclease III specific for double-stranded ribonucleic acid
    • 235898 1:CAS:528:DyaE28XitFek 1100606
    • Apirion D, Watson N (1975) Mapping and characterization of a mutation in Escherichia coli that reduces the level of ribonuclease III specific for double-stranded ribonucleic acid. J Bacteriol 124(1):317-324
    • (1975) J Bacteriol , vol.124 , Issue.1 , pp. 317-324
    • Apirion, D.1    Watson, N.2
  • 6
    • 0017800890 scopus 로고
    • Ribonuclease III is involved in motility of Escherichia coli
    • 222203 1:CAS:528:DyaE1cXhvVGqu7g%3D 346582
    • Apirion D, Watson N (1978) Ribonuclease III is involved in motility of Escherichia coli. J Bacteriol 133(3):1543-1545
    • (1978) J Bacteriol , vol.133 , Issue.3 , pp. 1543-1545
    • Apirion, D.1    Watson, N.2
  • 7
    • 0005987590 scopus 로고
    • Properties of a mutant from Synechocystis PCC6803 Resistant to acetazolamide, an inhibitor of carbonic anhydrase
    • 1062673 1:CAS:528:DyaK3cXls1yks7c%3D 16667618
    • Bedu S, Peltier G, Sarrey F, Joset F (1990) Properties of a mutant from Synechocystis PCC6803 Resistant to acetazolamide, an inhibitor of carbonic anhydrase. Plant Physiol 93(4):1312-1315
    • (1990) Plant Physiol , vol.93 , Issue.4 , pp. 1312-1315
    • Bedu, S.1    Peltier, G.2    Sarrey, F.3    Joset, F.4
  • 9
    • 0029240497 scopus 로고
    • A protein is involved in accessibility of the inhibitor acetazolamide to the carbonic anhydrase(s) in the cyanobacterium Synechocystis PCC 6803
    • 1:CAS:528:DyaK2MXlt1Wnu7k%3D 7727754
    • Beuf L, Bedu S, Cami B, Joset F (1995) A protein is involved in accessibility of the inhibitor acetazolamide to the carbonic anhydrase(s) in the cyanobacterium Synechocystis PCC 6803. Plant Mol Biol 27(4):779-788
    • (1995) Plant Mol Biol , vol.27 , Issue.4 , pp. 779-788
    • Beuf, L.1    Bedu, S.2    Cami, B.3    Joset, F.4
  • 11
    • 0028269435 scopus 로고
    • Copurification of Escherichia coli RNAase e and PNPase: Evidence for a specific association between two enzymes important in RNA processing and degradation
    • 1:CAS:528:DyaK2cXkt12ltr0%3D 7510217
    • Carpousis AJ, Vanhouwe G, Ehretsmann C, Krisch HM (1994) Copurification of Escherichia coli RNAase E and PNPase: evidence for a specific association between two enzymes important in RNA processing and degradation. Cell 76(5):889-900
    • (1994) Cell , vol.76 , Issue.5 , pp. 889-900
    • Carpousis, A.J.1    Vanhouwe, G.2    Ehretsmann, C.3    Krisch, H.M.4
  • 13
    • 34250875706 scopus 로고    scopus 로고
    • Initiation of RNA decay in Escherichia coli by 5′ pyrophosphate removal
    • 2196405 1:CAS:528:DC%2BD2sXot1els7k%3D 17612492
    • Celesnik H, Deana A, Belasco JG (2007) Initiation of RNA decay in Escherichia coli by 5′ pyrophosphate removal. Mol Cell 27(1):79-90
    • (2007) Mol Cell , vol.27 , Issue.1 , pp. 79-90
    • Celesnik, H.1    Deana, A.2    Belasco, J.G.3
  • 14
    • 34248575624 scopus 로고    scopus 로고
    • Specialized techniques for site-directed mutagenesis in cyanobacteria
    • 1:CAS:528:DC%2BD2sXjtlGqsr4%3D 17417008
    • Clerico EM, Ditty JL, Golden SS (2007) Specialized techniques for site-directed mutagenesis in cyanobacteria. Methods Mol Biol 362:155-171
    • (2007) Methods Mol Biol , vol.362 , pp. 155-171
    • Clerico, E.M.1    Ditty, J.L.2    Golden, S.S.3
  • 15
    • 77955412028 scopus 로고    scopus 로고
    • What is the role of RNase J in mRNA turnover?
    • 1:CAS:528:DC%2BC3cXhsVKlurfM 20458164
    • Condon C (2010) What is the role of RNase J in mRNA turnover? RNA Biol 7(3):316-321
    • (2010) RNA Biol , vol.7 , Issue.3 , pp. 316-321
    • Condon, C.1
  • 16
    • 0037115876 scopus 로고    scopus 로고
    • The phylogenetic distribution of bacterial ribonucleases
    • 140075 1:CAS:528:DC%2BD3sXlt1Sgsw%3D%3D 12490701
    • Condon C, Putzer H (2002) The phylogenetic distribution of bacterial ribonucleases. Nucleic Acids Res 30(24):5339-5346
    • (2002) Nucleic Acids Res , vol.30 , Issue.24 , pp. 5339-5346
    • Condon, C.1    Putzer, H.2
  • 18
    • 2142738304 scopus 로고    scopus 로고
    • WebLogo: A sequence logo generator
    • 419797 1:CAS:528:DC%2BD2cXkvFGht7Y%3D 15173120
    • Crooks GE, Hon G, Chandonia JM, Brenner SE (2004) WebLogo: a sequence logo generator. Genome Res 14(6):1188-1190
    • (2004) Genome Res , vol.14 , Issue.6 , pp. 1188-1190
    • Crooks, G.E.1    Hon, G.2    Chandonia, J.M.3    Brenner, S.E.4
  • 19
    • 38349117689 scopus 로고    scopus 로고
    • The bacterial enzyme RppH triggers messenger RNA degradation by 5′ pyrophosphate removal
    • 1:CAS:528:DC%2BD1cXnt1Gisw%3D%3D 18202662
    • Deana A, Celesnik H, Belasco JG (2008) The bacterial enzyme RppH triggers messenger RNA degradation by 5′ pyrophosphate removal. Nature 451(7176):355-358
    • (2008) Nature , vol.451 , Issue.7176 , pp. 355-358
    • Deana, A.1    Celesnik, H.2    Belasco, J.G.3
  • 21
    • 33646471951 scopus 로고    scopus 로고
    • An internal antisense RNA regulates expression of the photosynthesis gene isiA
    • 1459017 16636284
    • Duhring U, Axmann IM, Hess WR, Wilde A (2006) An internal antisense RNA regulates expression of the photosynthesis gene isiA. Proc Natl Acad Sci USA 103(18):7054-7058
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.18 , pp. 7054-7058
    • Duhring, U.1    Axmann, I.M.2    Hess, W.R.3    Wilde, A.4
  • 22
    • 84872010039 scopus 로고    scopus 로고
    • The essential function of B subtilis RNase III is to silence foreign toxin genes
    • 3531473 1:CAS:528:DC%2BC3sXhtFalurc%3D 23300471
    • Durand S, Gilet L, Condon C (2012) The essential function of B. subtilis RNase III is to silence foreign toxin genes. PLoS Genet 8(12):e1003181
    • (2012) PLoS Genet , vol.8 , Issue.12 , pp. e1003181
    • Durand, S.1    Gilet, L.2    Condon, C.3
  • 23
    • 84866931878 scopus 로고    scopus 로고
    • The antisense RNA As1-flv4 in the Cyanobacterium Synechocystis sp. PCC 6803 prevents premature expression of the flv4-2 operon upon shift in inorganic carbon supply
    • 3460422 1:CAS:528:DC%2BC38XhsVarsL3M 22854963
    • Eisenhut M, Georg J, Klahn S, Sakurai I, Mustila H, Zhang P, Hess WR, Aro EM (2012) The antisense RNA As1-flv4 in the Cyanobacterium Synechocystis sp. PCC 6803 prevents premature expression of the flv4-2 operon upon shift in inorganic carbon supply. J Biol Chem 287(40):33153-33162
    • (2012) J Biol Chem , vol.287 , Issue.40 , pp. 33153-33162
    • Eisenhut, M.1    Georg, J.2    Klahn, S.3    Sakurai, I.4    Mustila, H.5    Zhang, P.6    Hess, W.R.7    Aro, E.M.8
  • 24
    • 17844361922 scopus 로고    scopus 로고
    • Ribonucleases J1 and J2: Two novel endoribonucleases in B subtilis with functional homology to E coli RNase e
    • 1079966 1:CAS:528:DC%2BD2MXjsl2gs74%3D 15831787
    • Even S, Pellegrini O, Zig L, Labas V, Vinh J, Brechemmier-Baey D, Putzer H (2005) Ribonucleases J1 and J2: two novel endoribonucleases in B. subtilis with functional homology to E. coli RNase E. Nucleic Acids Res 33(7):2141-2152
    • (2005) Nucleic Acids Res , vol.33 , Issue.7 , 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
  • 25
    • 84879505615 scopus 로고    scopus 로고
    • RNase III-dependent down-regulation of ftsH by an artificial internal sense RNA in Anabaena sp. PCC 7120
    • 1:CAS:528:DC%2BC3sXhtFOqsL7J 23617281
    • Gao Y, Gong Y, Xu X (2013) RNase III-dependent down-regulation of ftsH by an artificial internal sense RNA in Anabaena sp. PCC 7120. FEMS Microbiol Lett 344(2):130-137
    • (2013) FEMS Microbiol Lett , vol.344 , Issue.2 , pp. 130-137
    • Gao, Y.1    Gong, Y.2    Xu, X.3
  • 27
    • 67349270900 scopus 로고    scopus 로고
    • Enzymatic assembly of DNA molecules up to several hundred kilobases
    • 1:CAS:528:DC%2BD1MXksVemsbw%3D 19363495
    • Gibson DG, Young L, Chuang RY, Venter JC, Hutchison CA, Smith HO (2009) Enzymatic assembly of DNA molecules up to several hundred kilobases. Nat Methods 6(5):343-345
    • (2009) Nat Methods , vol.6 , Issue.5 , pp. 343-345
    • Gibson, D.G.1    Young, L.2    Chuang, R.Y.3    Venter, J.C.4    Hutchison, C.A.5    Smith, H.O.6
  • 28
    • 0032578486 scopus 로고    scopus 로고
    • The endoribonucleolytic N-terminal half of Escherichia coli RNase e is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly
    • 21693 1:CAS:528:DyaK1cXmsV2iu78%3D 9751718
    • Kaberdin VR, Miczak A, Jakobsen JS, Lin-Chao S, McDowall KJ, von Gabain A (1998) The endoribonucleolytic N-terminal half of Escherichia coli RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly. Proc Natl Acad Sci USA 95(20):11637-11642
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.20 , pp. 11637-11642
    • Kaberdin, V.R.1    Miczak, A.2    Jakobsen, J.S.3    Lin-Chao, S.4    McDowall, K.J.5    Von Gabain, A.6
  • 29
    • 0029889965 scopus 로고    scopus 로고
    • RNase e polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli
    • 232654 1:CAS:528:DyaK28XjvFegt70%3D 8682798
    • Kido M, Yamanaka K, Mitani T, Niki H, Ogura T, Hiraga S (1996) RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli. J Bacteriol 178(13):3917-3925
    • (1996) J Bacteriol , vol.178 , Issue.13 , pp. 3917-3925
    • Kido, M.1    Yamanaka, K.2    Mitani, T.3    Niki, H.4    Ogura, T.5    Hiraga, S.6
  • 30
    • 77951539769 scopus 로고    scopus 로고
    • Rapid cleavage of RNA by RNase e in the absence of 5′ monophosphate stimulation
    • 2948425 1:CAS:528:DC%2BC3cXmsF2msbc%3D 19889093
    • Kime L, Jourdan SS, Stead JA, Hidalgo-Sastre A, McDowall KJ (2010) Rapid cleavage of RNA by RNase E in the absence of 5′ monophosphate stimulation. Mol Microbiol 76(3):590-604
    • (2010) Mol Microbiol , vol.76 , Issue.3 , pp. 590-604
    • Kime, L.1    Jourdan, S.S.2    Stead, J.A.3    Hidalgo-Sastre, A.4    McDowall, K.J.5
  • 31
    • 0036047092 scopus 로고    scopus 로고
    • Function in Escherichia coli of the non-catalytic part of RNase E: Role in the degradation of ribosome-free mRNA
    • 1:CAS:528:DC%2BD38XntFGktLg%3D 12207692
    • Leroy A, Vanzo NF, Sousa S, Dreyfus M, Carpousis AJ (2002) Function in Escherichia coli of the non-catalytic part of RNase E: role in the degradation of ribosome-free mRNA. Mol Microbiol 45(5):1231-1243
    • (2002) Mol Microbiol , vol.45 , Issue.5 , pp. 1231-1243
    • Leroy, A.1    Vanzo, N.F.2    Sousa, S.3    Dreyfus, M.4    Carpousis, A.J.5
  • 32
    • 84888986750 scopus 로고    scopus 로고
    • Key events during the transition from rapid growth to quiescence in budding yeast require posttranscriptional regulators
    • 3842996 1:CAS:528:DC%2BC3sXhvVygsr%2FJ 24088570
    • Li L, Miles S, Melville Z, Prasad A, Bradley G, Breeden LL (2013) Key events during the transition from rapid growth to quiescence in budding yeast require posttranscriptional regulators. Mol Biol Cell 24(23):3697-3709
    • (2013) Mol Biol Cell , vol.24 , Issue.23 , pp. 3697-3709
    • Li, L.1    Miles, S.2    Melville, Z.3    Prasad, A.4    Bradley, G.5    Breeden, L.L.6
  • 33
    • 84871321022 scopus 로고    scopus 로고
    • RNase E: At the interface of bacterial RNA processing and decay
    • 1:CAS:528:DC%2BC38XhvVersr%2FL 23241849
    • Mackie GA (2013) RNase E: at the interface of bacterial RNA processing and decay. Nat Rev Microbiol 11(1):45-57
    • (2013) Nat Rev Microbiol , vol.11 , Issue.1 , pp. 45-57
    • Mackie, G.A.1
  • 34
    • 34249101864 scopus 로고    scopus 로고
    • 5′-to-3′ exoribonuclease activity in bacteria: Role of RNase J1 in rRNA maturation and 5′ stability of mRNA
    • 1:CAS:528:DC%2BD2sXmtFGqu7w%3D 17512403
    • Mathy N, Benard L, Pellegrini O, Daou R, Wen T, Condon C (2007) 5′-to-3′ exoribonuclease activity in bacteria: role of RNase J1 in rRNA maturation and 5′ stability of mRNA. Cell 129(4):681-692
    • (2007) Cell , vol.129 , Issue.4 , pp. 681-692
    • Mathy, N.1    Benard, L.2    Pellegrini, O.3    Daou, R.4    Wen, T.5    Condon, C.6
  • 35
    • 84857769171 scopus 로고    scopus 로고
    • The rnb gene of Synechocystis PCC6803 encodes a RNA hydrolase displaying RNase II and not RNase R enzymatic properties
    • 3293843 1:CAS:528:DC%2BC38XjvFaisrg%3D 22403697
    • Matos RG, Fialho AM, Giloh M, Schuster G, Arraiano CM (2012) The rnb gene of Synechocystis PCC6803 encodes a RNA hydrolase displaying RNase II and not RNase R enzymatic properties. PLoS One 7(3):e32690
    • (2012) PLoS One , vol.7 , Issue.3 , pp. e32690
    • Matos, R.G.1    Fialho, A.M.2    Giloh, M.3    Schuster, G.4    Arraiano, C.M.5
  • 37
    • 0029976430 scopus 로고    scopus 로고
    • Proteins associated with RNase e in a multicomponent ribonucleolytic complex
    • 39450 1:CAS:528:DyaK28XivVKrtrY%3D 8632981
    • Miczak A, Kaberdin VR, Wei CL, Lin-Chao S (1996) Proteins associated with RNase E in a multicomponent ribonucleolytic complex. Proc Natl Acad Sci USA 93(9):3865-3869
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.9 , pp. 3865-3869
    • Miczak, A.1    Kaberdin, V.R.2    Wei, C.L.3    Lin-Chao, S.4
  • 38
    • 0018582283 scopus 로고
    • RNase E, an RNA processing enzyme from Escherichia coli
    • 1:CAS:528:DyaL3cXhslOlsA%3D%3D 387765
    • Misra TK, Apirion D (1979) RNase E, an RNA processing enzyme from Escherichia coli. J Biol Chem 254(21):11154-11159
    • (1979) J Biol Chem , vol.254 , Issue.21 , pp. 11154-11159
    • Misra, T.K.1    Apirion, D.2
  • 39
    • 58249086415 scopus 로고    scopus 로고
    • Analysis of RNA Decay, processing, and polyadenylation in Escherichia coli and other prokaryotes
    • 1:CAS:528:DC%2BD1MXhslWjsbY%3D
    • Mohanty BK, Giladi H, Maples VF, Kushner SR (2008) Analysis of RNA Decay, processing, and polyadenylation in Escherichia coli and other prokaryotes. RNA Turnover Bact Archaea Organelles 447:3-29
    • (2008) RNA Turnover Bact Archaea Organelles , vol.447 , pp. 3-29
    • Mohanty, B.K.1    Giladi, H.2    Maples, V.F.3    Kushner, S.R.4
  • 40
    • 0025091816 scopus 로고
    • Nucleotide sequence and further characterization of the Synechococcus sp strain PCC 7002 recA gene: Complementation of a cyanobacterial recA mutation by the Escherichia coli recA gene
    • Murphy RC, Gasparich GE, Bryant DA, Porter RD (1990) Nucleotide sequence and further characterization of the Synechococcus sp. strain PCC 7002 recA gene: complementation of a cyanobacterial recA mutation by the Escherichia coli recA gene. J Bacteriol 172(2):967-976
    • (1990) J Bacteriol , vol.172 , Issue.2 , pp. 967-976
    • Murphy, R.C.1    Gasparich, G.E.2    Bryant, D.A.3    Porter, R.D.4
  • 41
    • 0042665928 scopus 로고    scopus 로고
    • RNase G of Escherichia coli exhibits only limited functional overlap with its essential homologue, RNase e
    • 1:CAS:528:DC%2BD3sXmtFekt7k%3D 12864847
    • Ow MC, Perwez T, Kushner SR (2003) RNase G of Escherichia coli exhibits only limited functional overlap with its essential homologue, RNase E. Mol Microbiol 49(3):607-622
    • (2003) Mol Microbiol , vol.49 , Issue.3 , pp. 607-622
    • Ow, M.C.1    Perwez, T.2    Kushner, S.R.3
  • 43
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • 1:CAS:528:DyaK28XivVyks70%3D 8610017
    • Py B, Higgins CF, Krisch HM, Carpousis AJ (1996) A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature 381(6578):169-172
    • (1996) Nature , vol.381 , Issue.6578 , pp. 169-172
    • Py, B.1    Higgins, C.F.2    Krisch, H.M.3    Carpousis, A.J.4
  • 44
    • 43449118061 scopus 로고    scopus 로고
    • Mini-III, an unusual member of the RNase III family of enzymes, catalyses 23S ribosomal RNA maturation in B subtilis
    • 1:CAS:528:DC%2BD1cXntVemtLk%3D 18363798
    • Redko Y, Bechhofer DH, Condon C (2008) Mini-III, an unusual member of the RNase III family of enzymes, catalyses 23S ribosomal RNA maturation in B. subtilis. Mol Microbiol 68(5):1096-1106
    • (2008) Mol Microbiol , vol.68 , Issue.5 , pp. 1096-1106
    • Redko, Y.1    Bechhofer, D.H.2    Condon, C.3
  • 45
    • 0038182527 scopus 로고    scopus 로고
    • RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli
    • 1:CAS:528:DC%2BD3sXjt1ehsrs%3D 12601000
    • Rott R, Zipor G, Portnoy V, Liveanu V, Schuster G (2003) RNA polyadenylation and degradation in cyanobacteria are similar to the chloroplast but different from Escherichia coli. J Biol Chem 278(18):15771-15777
    • (2003) J Biol Chem , vol.278 , Issue.18 , pp. 15771-15777
    • Rott, R.1    Zipor, G.2    Portnoy, V.3    Liveanu, V.4    Schuster, G.5
  • 46
    • 84867135315 scopus 로고    scopus 로고
    • Positive regulation of psbA gene expression by cis-encoded antisense RNAs in synechocystis sp. PCC 6803
    • 3461525 1:CAS:528:DC%2BC38XhsFaksbfP 22858634
    • Sakurai I, Stazic D, Eisenhut M, Vuorio E, Steglich C, Hess WR, Aro EM (2012) Positive regulation of psbA gene expression by cis-encoded antisense RNAs in synechocystis sp. PCC 6803. Plant Physiol 160(2):1000-1010
    • (2012) Plant Physiol , vol.160 , Issue.2 , pp. 1000-1010
    • Sakurai, I.1    Stazic, D.2    Eisenhut, M.3    Vuorio, E.4    Steglich, C.5    Hess, W.R.6    Aro, E.M.7
  • 47
    • 70450222923 scopus 로고    scopus 로고
    • RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis
    • 2782095 1:CAS:528:DC%2BD1MXhtFOhsrfP 19779461
    • Shahbabian K, Jamalli A, Zig L, Putzer H (2009) RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis. EMBO J 28(22):3523-3533
    • (2009) EMBO J , vol.28 , Issue.22 , pp. 3523-3533
    • Shahbabian, K.1    Jamalli, A.2    Zig, L.3    Putzer, H.4
  • 49
    • 84980313965 scopus 로고
    • The production of hydrogen peroxide by blue-green algae: A survey
    • 1:CAS:528:DyaE2cXktlGhurc%3D
    • Stevens SEJ, Patterson COP, Meyers J (1973) The production of hydrogen peroxide by blue-green algae: a survey. J Phycol 9:427-430
    • (1973) J Phycol , vol.9 , pp. 427-430
    • Stevens, S.E.J.1    Patterson, C.O.P.2    Meyers, J.3
  • 50
    • 3543037550 scopus 로고    scopus 로고
    • Ribonuclease e organizes the protein interactions in the Escherichia coli RNA degradosome
    • 317140 1:CAS:528:DyaK1cXlvFOitrc%3D 9732274
    • Vanzo NF, Li YS, Py B, Blum E, Higgins CF, Raynal LC, Krisch HM, Carpousis AJ (1998) Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome. Genes Dev 12(17):2770-2781
    • (1998) Genes Dev , vol.12 , Issue.17 , pp. 2770-2781
    • Vanzo, N.F.1    Li, Y.S.2    Py, B.3    Blum, E.4    Higgins, C.F.5    Raynal, L.C.6    Krisch, H.M.7    Carpousis, A.J.8
  • 51
    • 84896518255 scopus 로고    scopus 로고
    • RNase e forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region
    • 3964918 1:CAS:528:DC%2BC2cXlvFCmur8%3D 24563514
    • Zhang JY, Deng XM, Li FP, Wang L, Huang QY, Zhang CC, Chen WL (2014) RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria via a cyanobacterial-specific nonapeptide in the noncatalytic region. RNA 20(4):568-579
    • (2014) RNA , vol.20 , Issue.4 , pp. 568-579
    • Zhang, J.Y.1    Deng, X.M.2    Li, F.P.3    Wang, L.4    Huang, Q.Y.5    Zhang, C.C.6    Chen, W.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.