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Volumn 8, Issue 11, 2013, Pages

Transcriptional and proteolytic regulation of the toxin- Antitoxin locus vapBC10 (ssr2962/slr1767) on the chromosome of synechocystis sp. PCC 6803

Author keywords

[No Author keywords available]

Indexed keywords

ANTITOXIN; BACTERIAL TOXIN; PROTEIN CLPXP; PROTEINASE; UNCLASSIFIED DRUG;

EID: 84896691925     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0080716     Document Type: Article
Times cited : (12)

References (49)
  • 1
    • 0022390750 scopus 로고
    • Effects of the ccd function of the F plasmid on bacterial growth
    • Jaffe A, Ogura T, Hiraga S (1985) Effects of the ccd function of the F plasmid on bacterial growth. J Bacteriol 163: 841-849. (Pubitemid 15230711)
    • (1985) Journal of Bacteriology , vol.163 , Issue.3 , pp. 841-849
    • Jaffe, A.1    Ogura, T.2    Hiraga, S.3
  • 2
    • 14244266086 scopus 로고    scopus 로고
    • Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes
    • DOI 10.1093/nar/gki201
    • Pandey DP, Gerdes K (2005) Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes. Nucleic Acids Res 33: 966-976. (Pubitemid 41430517)
    • (2005) Nucleic Acids Research , vol.33 , Issue.3 , pp. 966-976
    • Pandey, D.P.1    Gerdes, K.2
  • 3
    • 67649933665 scopus 로고    scopus 로고
    • Comprehensive comparative-genomic analysis of Type 2 toxin-antitoxin systems and related mobile stress response systems in prokaryotes
    • doi:10.1186/1745-6150-1184-1119
    • Makarova K, Wolf Y, Koonin E (2009) Comprehensive comparative-genomic analysis of Type 2 toxin-antitoxin systems and related mobile stress response systems in prokaryotes. Biol Direct 4: doi:10.1186/1745-6150-1184-1119.
    • (2009) Biol Direct , vol.4
    • Makarova, K.1    Wolf, Y.2    Koonin, E.3
  • 4
    • 80052196405 scopus 로고    scopus 로고
    • Diversity of bacterial type II toxin-antitoxin systems: A comprehensive search and functional analysis of novel families
    • Leplae R, Geeraerts D, Hallez R, Guglielmini J, Dreze P, et al. (2011) Diversity of bacterial type II toxin-antitoxin systems: a comprehensive search and functional analysis of novel families. Nucleic Acids Res 39: 5513-5525.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5513-5525
    • Leplae, R.1    Geeraerts, D.2    Hallez, R.3    Guglielmini, J.4    Dreze, P.5
  • 5
    • 34548488930 scopus 로고    scopus 로고
    • Hypothetical functions of toxin-antitoxin systems
    • Magnuson RD (2007) Hypothetical functions of toxin-antitoxin systems. J Bacteriol 189: 6089-6092.
    • (2007) J Bacteriol , vol.189 , pp. 6089-6092
    • Magnuson, R.D.1
  • 6
    • 63449102873 scopus 로고    scopus 로고
    • Bacterial toxin-antitoxin systems: More than selfish entities?
    • Van Melderen L, Saavedra De Bast M (2009) Bacterial toxin-antitoxin systems: more than selfish entities? PLoS Genet 5: e1000437.
    • (2009) PLoS Genet , vol.5
    • Van Melderen, L.1    Saavedra De Bast, M.2
  • 7
    • 84874212005 scopus 로고    scopus 로고
    • Toxin-antitoxin systems are ubiquitous and versatile modulators of prokaryotic cell fate
    • Schuster CF, Bertram R (2013) Toxin-antitoxin systems are ubiquitous and versatile modulators of prokaryotic cell fate. FEMS Microbiol Lett 340: 73-85.
    • (2013) FEMS Microbiol Lett , vol.340 , pp. 73-85
    • Schuster, C.F.1    Bertram, R.2
  • 8
    • 70350399514 scopus 로고    scopus 로고
    • MqsR, a crucial regulator for quorum sensing and biofilm formation, is a GCU-specific mRNA interferase in Escherichia coli
    • Yamaguchi Y, Park JH, Inouye M (2009) MqsR, a crucial regulator for quorum sensing and biofilm formation, is a GCU-specific mRNA interferase in Escherichia coli. J Biol Chem 284: 28746-28753.
    • (2009) J Biol Chem , vol.284 , pp. 28746-28753
    • Yamaguchi, Y.1    Park, J.H.2    Inouye, M.3
  • 9
    • 0041825422 scopus 로고    scopus 로고
    • Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA
    • DOI 10.1016/S0022-2836(03)00922-7
    • Christensen SK, Pedersen K, Hansen FG, Gerdes K (2003) Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA. J Mol Biol 332: 809-819. (Pubitemid 37101369)
    • (2003) Journal of Molecular Biology , vol.332 , Issue.4 , pp. 809-819
    • Christensen, S.K.1    Pedersen, K.2    Hansen, F.G.3    Gerdes, K.4
  • 10
    • 33749178742 scopus 로고    scopus 로고
    • Two higBA loci in the Vibrio cholerae superintegron encode mRNA cleaving enzymes and can stabilize plasmids
    • DOI 10.1111/j.1365-2958.2006.05385.x
    • Christensen-Dalsgaard M, Gerdes K (2006) Two higBA loci in the Vibrio cholerae superintegron encode mRNA cleaving enzymes and can stabilize plasmids. Mol Microbiol 62: 397-411. (Pubitemid 44477230)
    • (2006) Molecular Microbiology , vol.62 , Issue.2 , pp. 397-411
    • Christensen-Dalsgaard, M.1    Gerdes, K.2
  • 11
    • 60849121408 scopus 로고    scopus 로고
    • HicA of Escherichia coli defines a novel family of translation- independent mRNA interferases in bacteria and archaea
    • Jørgensen MG, Pandey DP, Jaskolska M, Gerdes K (2009) HicA of Escherichia coli defines a novel family of translation-independent mRNA interferases in bacteria and archaea. J Bacteriol 191: 1191-1199.
    • (2009) J Bacteriol , vol.191 , pp. 1191-1199
    • Jørgensen, M.G.1    Pandey, D.P.2    Jaskolska, M.3    Gerdes, K.4
  • 12
    • 0037428226 scopus 로고    scopus 로고
    • The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site
    • DOI 10.1016/S0092-8674(02)01248-5
    • Pedersen K, Zavialov AV, Pavlov MY, Elf J, Gerdes K, et al. (2003) The bacterial toxin RelE displays codon-specific cleavage of mRNAs in the ribosomal A site. Cell 112: 131-140. (Pubitemid 36106425)
    • (2003) Cell , vol.112 , Issue.1 , pp. 131-140
    • Pedersen, K.1    Zavialov, A.V.2    Pavlov, M.Yu.3    Elf, J.4    Gerdes, K.5    Ehrenberg, M.6
  • 13
    • 60649093164 scopus 로고    scopus 로고
    • Bacterial toxin YafQ is an endoribonuclease that associates with the ribosome and blocks translation elongation through sequence-specific and frame-dependent mRNA cleavage
    • Prysak MH, Mozdzierz CJ, Cook AM, Zhu L, Zhang Y, et al. (2009) Bacterial toxin YafQ is an endoribonuclease that associates with the ribosome and blocks translation elongation through sequence-specific and frame-dependent mRNA cleavage. Mol Microbiol 71: 1071-1087.
    • (2009) Mol Microbiol , vol.71 , pp. 1071-1087
    • Prysak, M.H.1    Mozdzierz, C.J.2    Cook, A.M.3    Zhu, L.4    Zhang, Y.5
  • 15
    • 1542472730 scopus 로고    scopus 로고
    • New connections in the prokaryotic toxin-antitoxin network: Relationship with the eukaryotic nonsense-mediated RNA decay system
    • Anantharaman V, Aravind L (2003) New connections in the prokaryotic toxin-antitoxin network: relationship with the eukaryotic nonsense-mediated RNA decay system. Genome Biol 4: R81.
    • (2003) Genome Biol , vol.4
    • Anantharaman, V.1    Aravind, L.2
  • 16
    • 80054759036 scopus 로고    scopus 로고
    • Regulation of growth and death in Escherichia coli by toxin-antitoxin systems
    • Yamaguchi Y, Inouye M (2011) Regulation of growth and death in Escherichia coli by toxin-antitoxin systems. Nat Rev Microbiol 9: 779-790.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 779-790
    • Yamaguchi, Y.1    Inouye, M.2
  • 17
    • 0036067108 scopus 로고    scopus 로고
    • Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins
    • DOI 10.1046/j.1365-2958.2002.03027.x
    • Pedersen K, Christensen S, Gerdes K (2002) Rapid induction and reversal of a bacteriostatic condition by controlled expression of toxins and antitoxins. Mol Microbiol 45: 501-510. (Pubitemid 34779839)
    • (2002) Molecular Microbiology , vol.45 , Issue.2 , pp. 501-510
    • Pedersen, K.1    Christensen, S.K.2    Gerdes, K.3
  • 18
    • 10044283095 scopus 로고    scopus 로고
    • MazF-mediated cell death in Escherichia coli: A point of no return
    • DOI 10.1128/JB.186.24.8295-8300.2004
    • Amitai S, Yassin Y, Engelberg-Kulka H (2004) MazF-mediated cell death in Escherichia coli: a point of no return. J Bacteriol 186: 8295-8300. (Pubitemid 39603219)
    • (2004) Journal of Bacteriology , vol.186 , Issue.24 , pp. 8295-8300
    • Amitai, S.1    Yassin, Y.2    Engelberg-Kulka, H.3
  • 19
    • 37649005671 scopus 로고    scopus 로고
    • MazF, an mRNA interferase, mediates programmed cell death during multicellular Myxococcus development
    • Nariya H, Inouye M (2008) MazF, an mRNA interferase, mediates programmed cell death during multicellular Myxococcus development. Cell 132: 55-66.
    • (2008) Cell , vol.132 , pp. 55-66
    • Nariya, H.1    Inouye, M.2
  • 20
    • 84862783125 scopus 로고    scopus 로고
    • Artificial activation of toxin-antitoxin systems as an antibacterial strategy
    • Williams JJ, Hergenrother PJ (2012) Artificial activation of toxin-antitoxin systems as an antibacterial strategy. Trends Microbiol 20: 291-298.
    • (2012) Trends Microbiol , vol.20 , pp. 291-298
    • Williams, J.J.1    Hergenrother, P.J.2
  • 21
    • 78650444037 scopus 로고    scopus 로고
    • The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array
    • Arcus VL, McKenzie JL, Robson J, Cook GM (2011) The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array. Protein Eng Des Sel 24: 33-40.
    • (2011) Protein Eng des Sel , vol.24 , pp. 33-40
    • Arcus, V.L.1    McKenzie, J.L.2    Robson, J.3    Cook, G.M.4
  • 22
    • 78650444037 scopus 로고    scopus 로고
    • The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array
    • Arcus VL, McKenzie JL, Robson J, Cook GM (2011) The PIN-domain ribonucleases and the prokaryotic VapBC toxin-antitoxin array. Protein Eng Des Sel 24: 33-40.
    • (2011) Protein Eng des Sel , vol.24 , pp. 33-40
    • Arcus, V.L.1    McKenzie, J.L.2    Robson, J.3    Cook, G.M.4
  • 23
    • 79956328889 scopus 로고    scopus 로고
    • Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNA
    • Winther KS, Gerdes K (2011) Enteric virulence associated protein VapC inhibits translation by cleavage of initiator tRNA. Proc Natl Acad Sci U S A 108: 7403-7407.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 7403-7407
    • Winther, K.S.1    Gerdes, K.2
  • 24
    • 84861397933 scopus 로고    scopus 로고
    • Determination of ribonuclease sequence-specificity using Pentaprobes and mass spectrometry
    • McKenzie JL, Duyvestyn JM, Smith T, Bendak K, MacKay J, et al. (2012) Determination of ribonuclease sequence-specificity using Pentaprobes and mass spectrometry. RNA 18: 1267-1278.
    • (2012) RNA , vol.18 , pp. 1267-1278
    • McKenzie, J.L.1    Duyvestyn, J.M.2    Smith, T.3    Bendak, K.4    MacKay, J.5
  • 25
    • 84859783727 scopus 로고    scopus 로고
    • Growth andtranslation inhibition through sequence-specific RNA binding by Mycobacterium tuberculosis VapC Toxin
    • Sharp JD, Cruz JW, Raman S, Inouye M, Husson RN, et al. (2012) Growth andtranslation inhibition through sequence-specific RNA binding by Mycobacterium tuberculosis VapC Toxin. J Biol Chem 287: 12835-12847.
    • (2012) J Biol Chem , vol.287 , pp. 12835-12847
    • Sharp, J.D.1    Cruz, J.W.2    Raman, S.3    Inouye, M.4    Husson, R.N.5
  • 26
    • 37249085679 scopus 로고    scopus 로고
    • Expression of functional Bacillus SpoIISAB toxin-antitoxin modules in Escherichia coli
    • DOI 10.1111/j.1574-6968.2007.00984.x
    • Florek P, Muchova K, Pavelcikova P, Barak I (2008) Expression of functional Bacillus SpoIISAB toxin-antitoxin modules in Escherichia coli. FEMS Microbiol Lett 278: 177-184. (Pubitemid 350264574)
    • (2008) FEMS Microbiology Letters , vol.278 , Issue.2 , pp. 177-184
    • Florek, P.1    Muchova, K.2    Pavelcikova, P.3    Barak, I.4
  • 27
    • 39749130935 scopus 로고    scopus 로고
    • Biochemical characterization of a chromosomal toxin-antitoxin system in Mycobacterium tuberculosis
    • Zhao LX, Zhang JJ (2008) Biochemical characterization of a chromosomal toxin-antitoxin system in Mycobacterium tuberculosis . FEBS Lett 582: 710-714.
    • (2008) FEBS Lett , vol.582 , pp. 710-714
    • Zhao, L.X.1    Zhang, J.J.2
  • 28
    • 79951616353 scopus 로고    scopus 로고
    • The chromosomal mazEF Locus of Streptococcus mutans encodes a functional type II toxin-antitoxin addiction system
    • Syed MA, Koyanagi S, Sharma E, Jobin MC, Yakunin AF, et al. (2011) The chromosomal mazEF Locus of Streptococcus mutans encodes a functional type II toxin-antitoxin addiction system. J Bacteriol 193: 1122-1130.
    • (2011) J Bacteriol , vol.193 , pp. 1122-1130
    • Syed, M.A.1    Koyanagi, S.2    Sharma, E.3    Jobin, M.C.4    Yakunin, A.F.5
  • 29
    • 82755160777 scopus 로고    scopus 로고
    • The proteolytic activation of the relNEs (ssr1114/slr0664) toxin-antitoxin system by both proteases Lons and ClpP2s/Xs of Synechocystis sp. PCC 6803
    • Ning D, Ye S, Liu B, Chang J (2011) The proteolytic activation of the relNEs (ssr1114/slr0664) toxin-antitoxin system by both proteases Lons and ClpP2s/Xs of Synechocystis sp. PCC 6803. Curr Microbiol 63: 496-502.
    • (2011) Curr Microbiol , vol.63 , pp. 496-502
    • Ning, D.1    Ye, S.2    Liu, B.3    Chang, J.4
  • 30
    • 0025311083 scopus 로고
    • Use of a conditionally lethal gene in Anabaena sp. strain PCC 7120 to select for double recombinants and to entrap insertion sequences
    • Cai Y, Wolk CP (1990) Use of a conditionally lethal gene in Anabaena sp. strain PCC 7120 to select for double recombinants and to entrap insertions. J Bacteriol 172: 3138-3145. (Pubitemid 20179766)
    • (1990) Journal of Bacteriology , vol.172 , Issue.6 , pp. 3138-3145
    • Cai, Y.1    Wolk, C.P.2
  • 31
    • 48549096382 scopus 로고    scopus 로고
    • Construction of copper induced gene expression platform in Synechosystis sp. PCC6803
    • Gao H, Xu X (2007) Construction of copper induced gene expression platform in Synechosystis sp. PCC6803. Acta Hydrobiologica Sinica 31: 240-244.
    • (2007) Acta Hydrobiologica Sinica , vol.31 , pp. 240-244
    • Gao, H.1    Xu, X.2
  • 32
    • 1242296194 scopus 로고    scopus 로고
    • alr0117, a two-component histidine kinase gene, is involved in heterocyst development in Anabaena sp. PCC 7120
    • Ning D, Xu X (2004) alr0117, a two-component histidine kinase gene, is involved in heterocyst development in Anabaena sp. PCC 7120. Microbiology 150: 447-453. (Pubitemid 38220048)
    • (2004) Microbiology , vol.150 , Issue.2 , pp. 447-453
    • Ning, D.1    Xu, X.2
  • 33
    • 84874507920 scopus 로고    scopus 로고
    • Characterization of a chromosomal type II toxin-Antitoxin system mazEaFa in the cyanobacterium Anabaena sp PCC 7120
    • Ning DG, Jiang Y, Liu ZY, Xu QG (2013) Characterization of a chromosomal type II toxin-Antitoxin system mazEaFa in the cyanobacterium Anabaena sp PCC 7120. PLoS One 8(2):e56035.
    • (2013) PLoS One , vol.8 , Issue.2
    • Ning, D.G.1    Jiang, Y.2    Liu, Z.Y.3    Xu, Q.G.4
  • 35
    • 79952174199 scopus 로고    scopus 로고
    • An experimentally anchored map of transcriptional start sites in the model cyanobacterium Synechocystis sp PCC6803
    • Mitschke J, Georg J, Scholz I, Sharma CM, Dienst D, et al. (2011) An experimentally anchored map of transcriptional start sites in the model cyanobacterium Synechocystis sp PCC6803. Proc Natl Acad Sci U S A 108: 2124-2129.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 2124-2129
    • Mitschke, J.1    Georg, J.2    Scholz, I.3    Sharma, C.M.4    Dienst, D.5
  • 36
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • DOI 10.1002/prot.1168
    • Bates PA, Kelley LA, MacCallum RM, MJE S (2001) Enhancement of protein modelling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Protein Struct Funct Genet (Suppl) 5: 39-46. (Pubitemid 34113166)
    • (2001) Proteins: Structure, Function and Genetics , vol.45 , Issue.SUPPL. 5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.E.4
  • 37
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L, Rosenstrom P (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38: W545-549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 39
    • 0028230286 scopus 로고
    • The parDE operon of the broad-host-range plasmid RK2 specifies growth inhibition associated with plasmid loss
    • DOI 10.1006/jmbi.1994.1207
    • Roberts RC, Ström AR, Helinski DR (1994) The parDE operon of the broad-host-range plasmid RK2 specifies growth inhibition associated with plasmid loss. J Mol Biol 237: 35-51. (Pubitemid 24147467)
    • (1994) Journal of Molecular Biology , vol.237 , Issue.1 , pp. 35-51
    • Roberts, R.C.1    Strom, A.R.2    Helinski, D.R.3
  • 40
    • 0031982708 scopus 로고    scopus 로고
    • PinA inhibits ATP hydrolysis and energy-dependent protein degradation by Lon protease
    • DOI 10.1074/jbc.273.1.524
    • Hilliard JJ, Simon LD, Van Melderen L, Maurizi MR (1998) PinA inhibits ATP hydrolysis and energy-dependent protein degradation by Lon protease. J Biol Chem 273: 524-527. (Pubitemid 28042240)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.1 , pp. 524-527
    • Hilliard, J.J.1    Simon, L.D.2    Van Melderen, L.3    Maurizi, M.R.4
  • 41
    • 1542379603 scopus 로고    scopus 로고
    • The YefM antitoxin defines a family of natively unfolded proteins: Implications as a novel antibacterial target
    • DOI 10.1074/jbc.M308263200
    • Cherny I, Gazit E (2004) The YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target. J Biol Chem 279: 8252-8261. (Pubitemid 38294717)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 8252-8261
    • Cherny, I.1    Gazit, E.2
  • 42
    • 77749292157 scopus 로고    scopus 로고
    • Proteolytic regulation of toxin-antitoxin systems by ClpPC in Staphylococcus aureus
    • Donegan NP, Thompson ET, Fu Z, Cheung AL (2010) Proteolytic regulation of toxin-antitoxin systems by ClpPC in Staphylococcus aureus. J Bacteriol 192: 1416-1422.
    • (2010) J Bacteriol , vol.192 , pp. 1416-1422
    • Donegan, N.P.1    Thompson, E.T.2    Fu, Z.3    Cheung, A.L.4
  • 43
    • 84858128637 scopus 로고    scopus 로고
    • Regulation of the vapBC-1 Toxin-Antitoxin Locus in Nontypeable Haemophilus influenzae
    • Cline SD, Saleem S, Daines DA (2012) Regulation of the vapBC-1 Toxin-Antitoxin Locus in Nontypeable Haemophilus influenzae . PLoS One 7(3):e32199.
    • (2012) PLoS One , vol.7 , Issue.3
    • Cline, S.D.1    Saleem, S.2    Daines, D.A.3
  • 45
    • 0036068418 scopus 로고    scopus 로고
    • The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus
    • Schelin J, Lindmark F, Clarke A K. (2002) The clpP multigene family for the ATPdependent Clp protease in the cyanobacterium Synechococcus. Microbiology 14: 2255-2265. (Pubitemid 34785308)
    • (2002) Microbiology , vol.148 , Issue.7 , pp. 2255-2265
    • Schelin, J.1    Lindmark, F.2    Clarke, A.K.3
  • 46
    • 0032125857 scopus 로고    scopus 로고
    • Inactivation of the clpP1 gene for the proteolytic subunit of the ATP-dependent Clp protease in the cyanobacterium Synechococcus limits growth and light acclimation
    • DOI 10.1023/A:1006016302074
    • Clarke AK, Schelin J, Porankiewicz J (1998) Inactivation of the clpPI gene for the proteolytic subunit of the ATP-dependent Clp protease in the cyanobacterium Synechococcus limits growth and light acclimation. Plant Mol Biol 37: 791-801. (Pubitemid 28329437)
    • (1998) Plant Molecular Biology , vol.37 , Issue.5 , pp. 791-801
    • Clarke, A.K.1    Schelin, J.2    Porankiewicz, J.3
  • 47
    • 0031849161 scopus 로고    scopus 로고
    • The ATP-dependent Clp protease is essential for acclimation to UV-B and low temperature in the cyanobacterium Synechococcus
    • DOI 10.1046/j.1365-2958.1998.00928.x
    • Porankiewicz J, Schelin J, Clarke AK (1998) The ATP-dependent Clp protease is essential for acclimation to UV-B and low temperature in the cyanobacterium Synechococcus. Mol Microbiol 29: 275-283. (Pubitemid 28318580)
    • (1998) Molecular Microbiology , vol.29 , Issue.1 , pp. 275-283
    • Porankiewicz, J.1    Schelin, J.2    Clarke, A.K.3
  • 48
    • 0036068418 scopus 로고    scopus 로고
    • The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus
    • Schelin J, Lindmark F, Clarke AK (2002) The clpP multigene family for the ATP-dependent Clp protease in the cyanobacterium Synechococcus. Microbiology 148: 2255-2265. (Pubitemid 34785308)
    • (2002) Microbiology , vol.148 , Issue.7 , pp. 2255-2265
    • Schelin, J.1    Lindmark, F.2    Clarke, A.K.3
  • 49
    • 0030198323 scopus 로고    scopus 로고
    • The cyanobacterium Synechococcus sp. PCC 7942 possesses a close homologue to the chloroplast ClpC protein of higher plants
    • Clarke AK, Eriksson MJ (1996) The cyanobacterium Synechococcus sp. PCC 7942 possesses a close homologue to the chloroplast ClpC protein of higher plants. Plant Mol Biol 31: 721-730. (Pubitemid 26329921)
    • (1996) Plant Molecular Biology , vol.31 , Issue.4 , pp. 721-730
    • Clarke, A.K.1    Eriksson, M.-J.2


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