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Volumn 78, Issue 1-2, 2012, Pages 185-196

ppGpp inhibits peptide elongation cycle of chloroplast translation system in vitro

Author keywords

Antibiotics; Chloroplast; Elongation; In vitro translation; Pea; ppGpp

Indexed keywords

ANTIINFECTIVE AGENT; CARBON; DRUG DERIVATIVE; FUSIDIC ACID; GDPNP COMPOUND; GUANOSINE 3' DIPHOSPHATE 5' DIPHOSPHATE; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; LEUCINE; MESSENGER RNA; PEPTIDE; POLYPHENYLALANINE; POLYURIDYLIC ACID; THIOSTREPTON; VEGETABLE PROTEIN;

EID: 82755161750     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11103-011-9858-x     Document Type: Article
Times cited : (17)

References (56)
  • 2
    • 21644449199 scopus 로고    scopus 로고
    • Chloroplast elongation factor ts pro-protein is an evolutionarily conserved fusion with the s1 domain-containing plastid-specific ribosomal protein-7
    • Beligni MV, Yamaguchi K, Mayfield SP (2004) Chloroplast elongation factor ts pro-protein is an evolutionarily conserved fusion with the s1 domain-containing plastid-specific ribosomal protein-7. Plant Cell 16: 3357-3369.
    • (2004) Plant Cell , vol.16 , pp. 3357-3369
    • Beligni, M.V.1    Yamaguchi, K.2    Mayfield, S.P.3
  • 3
    • 0347635417 scopus 로고    scopus 로고
    • Photosynthetic eukaryotes unite: endosymbiosis connects the dots
    • Bhattacharya D, Yoon HS, Hackett JD (2004) Photosynthetic eukaryotes unite: endosymbiosis connects the dots. Bioessays 26: 50-60.
    • (2004) Bioessays , vol.26 , pp. 50-60
    • Bhattacharya, D.1    Yoon, H.S.2    Hackett, J.D.3
  • 5
    • 0035958953 scopus 로고    scopus 로고
    • A cDNA for nuclear-encoded chloroplast translational initiation factor 2 from a higher plant is able to complement an infB Escherichia coli null mutant
    • Campos F, Garcia-Gomez BI, Solorzano RM, Salazar E, Estevez J, Leon P, Alvarez-Buylla ER, Covarrubias AA (2001) A cDNA for nuclear-encoded chloroplast translational initiation factor 2 from a higher plant is able to complement an infB Escherichia coli null mutant. J Biol Chem 276: 28388-28394.
    • (2001) J Biol Chem , vol.276 , pp. 28388-28394
    • Campos, F.1    Garcia-Gomez, B.I.2    Solorzano, R.M.3    Salazar, E.4    Estevez, J.5    Leon, P.6    Alvarez-Buylla, E.R.7    Covarrubias, A.A.8
  • 6
    • 0014939550 scopus 로고
    • The control of ribonucleic acid synthesis in Escherichia coli
    • Cashel M, Kalbacher B (1970) The control of ribonucleic acid synthesis in Escherichia coli. J Biol Chem 245: 2309-2318.
    • (1970) J Biol Chem , vol.245 , pp. 2309-2318
    • Cashel, M.1    Kalbacher, B.2
  • 8
    • 70349651782 scopus 로고    scopus 로고
    • Multiple antibiotic resistance in Arabidopsis is conferred by mutations in a chloroplast-localized transport protein
    • Conte S, Stevenson D, Furner I, Lloyd A (2009) Multiple antibiotic resistance in Arabidopsis is conferred by mutations in a chloroplast-localized transport protein. Plant Physiol 151: 559-573.
    • (2009) Plant Physiol , vol.151 , pp. 559-573
    • Conte, S.1    Stevenson, D.2    Furner, I.3    Lloyd, A.4
  • 10
    • 79955651825 scopus 로고    scopus 로고
    • The chloroplast transformation toolbox: selectable markers and marker removal
    • Day A, Goldschmidt-Clermont M (2011) The chloroplast transformation toolbox: selectable markers and marker removal. Plant Biotechnol J 9: 540-553.
    • (2011) Plant Biotechnol J , vol.9 , pp. 540-553
    • Day, A.1    Goldschmidt-Clermont, M.2
  • 11
    • 0025108852 scopus 로고
    • In vitro synthesis of chlorophyll a in the dark triggers accumulation of chlorophyll a apoproteins in barley etioplasts
    • Eichacker LA, Soll J, Lauterbach P, Rudiger W, Klein RR, Mullet JE (1990) In vitro synthesis of chlorophyll a in the dark triggers accumulation of chlorophyll a apoproteins in barley etioplasts. J Biol Chem 265: 13566-13571.
    • (1990) J Biol Chem , vol.265 , pp. 13566-13571
    • Eichacker, L.A.1    Soll, J.2    Lauterbach, P.3    Rudiger, W.4    Klein, R.R.5    Mullet, J.E.6
  • 12
    • 0014696648 scopus 로고
    • Chloroplast ribosomes: stereospecificity of inhibition by chloramphenicol
    • Ellis RJ (1969) Chloroplast ribosomes: stereospecificity of inhibition by chloramphenicol. Science 163: 477-478.
    • (1969) Science , vol.163 , pp. 477-478
    • Ellis, R.J.1
  • 13
    • 0015137096 scopus 로고
    • Lincomycin as a chloroplast probe
    • Ellis RJ (1971) Lincomycin as a chloroplast probe. Biochem J 124: 52P-53P.
    • (1971) Biochem J , vol.124
    • Ellis, R.J.1
  • 14
    • 0006097480 scopus 로고
    • High rates of protein synthesis by isolated chloroplasts
    • Fish LE, Jagendorf AT (1982) High rates of protein synthesis by isolated chloroplasts. Plant Physiol 70: 1107-1114.
    • (1982) Plant Physiol , vol.70 , pp. 1107-1114
    • Fish, L.E.1    Jagendorf, A.T.2
  • 15
    • 70350602056 scopus 로고    scopus 로고
    • The structure of the ribosome with elongation factor G trapped in the posttranslocational state
    • Gao YG, Selmer M, Dunham CM, Weixlbaumer A, Kelley AC, Ramakrishnan V (2009) The structure of the ribosome with elongation factor G trapped in the posttranslocational state. Science 326: 694-699.
    • (2009) Science , vol.326 , pp. 694-699
    • Gao, Y.G.1    Selmer, M.2    Dunham, C.M.3    Weixlbaumer, A.4    Kelley, A.C.5    Ramakrishnan, V.6
  • 16
    • 1542320134 scopus 로고    scopus 로고
    • Inducible expression, enzymatic activity, and origin of higher plant homologues of bacterial RelA/SpoT stress proteins in Nicotiana tabacum
    • Givens RM, Lin MH, Taylor DJ, Mechold U, Berry JO, Hernandez VJ (2004) Inducible expression, enzymatic activity, and origin of higher plant homologues of bacterial RelA/SpoT stress proteins in Nicotiana tabacum. J Biol Chem 279: 7495-7504.
    • (2004) J Biol Chem , vol.279 , pp. 7495-7504
    • Givens, R.M.1    Lin, M.H.2    Taylor, D.J.3    Mechold, U.4    Berry, J.O.5    Hernandez, V.J.6
  • 17
    • 0015752570 scopus 로고
    • Role of guanine nucleotides in protein synthesis. Elongation factor G and guanosine 5′-triphosphate, 3′-diphosphate
    • Hamel E, Cashel M (1973) Role of guanine nucleotides in protein synthesis. Elongation factor G and guanosine 5′-triphosphate, 3′-diphosphate. Proc Natl Acad Sci U S A 70: 3250-3254.
    • (1973) Proc Natl Acad Sci U S A , vol.70 , pp. 3250-3254
    • Hamel, E.1    Cashel, M.2
  • 18
    • 0016250916 scopus 로고
    • Guanine nucleotides in protein synthesis. Utilization of pppGpp and dGTP by initiation factor 2 and elongation factor Tu
    • Hamel E, Cashel M (1974) Guanine nucleotides in protein synthesis. Utilization of pppGpp and dGTP by initiation factor 2 and elongation factor Tu. Arch Biochem Biophys 162: 293-300.
    • (1974) Arch Biochem Biophys , vol.162 , pp. 293-300
    • Hamel, E.1    Cashel, M.2
  • 21
    • 0027240238 scopus 로고
    • Cloning and sequencing of a soybean nuclear gene coding for a chloroplast translation elongation factor EF-G
    • Hernandez Torres J, Breitenberger CA, Spielmann A, Stutz E (1993) Cloning and sequencing of a soybean nuclear gene coding for a chloroplast translation elongation factor EF-G. Biochim Biophys Acta 1174: 191-194.
    • (1993) Biochim Biophys Acta , vol.1174 , pp. 191-194
    • Hernandez Torres, J.1    Breitenberger, C.A.2    Spielmann, A.3    Stutz, E.4
  • 22
    • 0029971659 scopus 로고    scopus 로고
    • Cis-acting elements and trans-acting factors for accurate translation of chloroplast psbA mRNAs: development of an in vitro translation system from tobacco chloroplasts
    • Hirose T, Sugiura M (1996) Cis-acting elements and trans-acting factors for accurate translation of chloroplast psbA mRNAs: development of an in vitro translation system from tobacco chloroplasts. EMBO J 15: 1687-1695.
    • (1996) EMBO J , vol.15 , pp. 1687-1695
    • Hirose, T.1    Sugiura, M.2
  • 23
    • 0002301235 scopus 로고
    • Further characterization of ribosome binding to thylakoid membranes
    • Hurewitz J, Jagendorf AT (1987) Further characterization of ribosome binding to thylakoid membranes. Plant Physiol 84: 31-34.
    • (1987) Plant Physiol , vol.84 , pp. 31-34
    • Hurewitz, J.1    Jagendorf, A.T.2
  • 24
    • 0037110760 scopus 로고    scopus 로고
    • A RelA-SpoT homolog (Cr-RSH) identified in Chlamydomonas reinhardtii generates stringent factor in vivo and localizes to chloroplasts in vitro
    • Kasai K, Usami S, Yamada T, Endo Y, Ochi K, Tozawa Y (2002) A RelA-SpoT homolog (Cr-RSH) identified in Chlamydomonas reinhardtii generates stringent factor in vivo and localizes to chloroplasts in vitro. Nucleic Acids Res 30: 4985-4992.
    • (2002) Nucleic Acids Res , vol.30 , pp. 4985-4992
    • Kasai, K.1    Usami, S.2    Yamada, T.3    Endo, Y.4    Ochi, K.5    Tozawa, Y.6
  • 25
    • 6344254432 scopus 로고    scopus 로고
    • Guanosine tetra- and pentaphosphate synthase activity in chloroplasts of a higher plant: association with 70S ribosomes and inhibition by tetracycline
    • Kasai K, Kanno T, Endo Y, Wakasa K, Tozawa Y (2004) Guanosine tetra- and pentaphosphate synthase activity in chloroplasts of a higher plant: association with 70S ribosomes and inhibition by tetracycline. Nucleic Acids Res 32: 5732-5741.
    • (2004) Nucleic Acids Res , vol.32 , pp. 5732-5741
    • Kasai, K.1    Kanno, T.2    Endo, Y.3    Wakasa, K.4    Tozawa, Y.5
  • 26
    • 0028388549 scopus 로고
    • Chlorophyll regulates accumulation of the plastid-encoded chlorophyll proteins P700 and D1 by increasing apoprotein stability
    • Kim J, Eichacker LA, Rudiger W, Mullet JE (1994) Chlorophyll regulates accumulation of the plastid-encoded chlorophyll proteins P700 and D1 by increasing apoprotein stability. Plant Physiol 104: 907-916.
    • (1994) Plant Physiol , vol.104 , pp. 907-916
    • Kim, J.1    Eichacker, L.A.2    Rudiger, W.3    Mullet, J.E.4
  • 27
    • 14444275280 scopus 로고
    • Inhibition of in vitro protein synthesis by ppGpp
    • Legault L, Jeantet C, Gros F (1972) Inhibition of in vitro protein synthesis by ppGpp. FEBS Lett 27: 71-75.
    • (1972) FEBS Lett , vol.27 , pp. 71-75
    • Legault, L.1    Jeantet, C.2    Gros, F.3
  • 28
    • 79955047348 scopus 로고    scopus 로고
    • Direct regulation of Escherichia coli ribosomal protein promoters by the transcription factors ppGpp and DksA
    • Lemke JJ, Sanchez-Vazquez P, Burgos HL, Hedberg G, Ross W, Gourse RL (2011) Direct regulation of Escherichia coli ribosomal protein promoters by the transcription factors ppGpp and DksA. Proc Natl Acad Sci U S A 108: 5712-5717.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 5712-5717
    • Lemke, J.J.1    Sanchez-Vazquez, P.2    Burgos, H.L.3    Hedberg, G.4    Ross, W.5    Gourse, R.L.6
  • 30
    • 38949215789 scopus 로고    scopus 로고
    • The bacterial stringent response, conserved in chloroplasts, controls plant fertilization
    • Masuda S, Mizusawa K, Narisawa T, Tozawa Y, Ohta H, Takamiya K (2008a) The bacterial stringent response, conserved in chloroplasts, controls plant fertilization. Plant Cell Physiol 49: 135-141.
    • (2008) Plant Cell Physiol , vol.49 , pp. 135-141
    • Masuda, S.1    Mizusawa, K.2    Narisawa, T.3    Tozawa, Y.4    Ohta, H.5    Takamiya, K.6
  • 31
    • 56049119193 scopus 로고    scopus 로고
    • Possible targets of "magic spots" in plant signalling
    • Masuda S, Tozawa Y, Ohta H (2008b) Possible targets of "magic spots" in plant signalling. Plant Signal Behav 3: 1021-1023.
    • (2008) Plant Signal Behav , vol.3 , pp. 1021-1023
    • Masuda, S.1    Tozawa, Y.2    Ohta, H.3
  • 34
    • 48749083049 scopus 로고    scopus 로고
    • Expression profiling of four RelA/SpoT-like proteins, homologues of bacterial stringent factors, in Arabidopsis thaliana
    • Mizusawa K, Masuda S, Ohta H (2008) Expression profiling of four RelA/SpoT-like proteins, homologues of bacterial stringent factors, in Arabidopsis thaliana. Planta 228: 553-562.
    • (2008) Planta , vol.228 , pp. 553-562
    • Mizusawa, K.1    Masuda, S.2    Ohta, H.3
  • 35
    • 0027651682 scopus 로고
    • Purification of chloroplast elongation factor Tu and cDNA analysis in tobacco: the existence of two chloroplast elongation factor Tu species
    • Murayama Y, Matsubayashi T, Sugita M, Sugiura M (1993) Purification of chloroplast elongation factor Tu and cDNA analysis in tobacco: the existence of two chloroplast elongation factor Tu species. Plant Mol Biol 22: 767-774.
    • (1993) Plant Mol Biol , vol.22 , pp. 767-774
    • Murayama, Y.1    Matsubayashi, T.2    Sugita, M.3    Sugiura, M.4
  • 36
    • 0035029364 scopus 로고    scopus 로고
    • Biological cost and compensatory evolution in fusidic acid-resistant Staphylococcus aureus
    • Nagaev I, Bjorkman J, Andersson DI, Hughes D (2001) Biological cost and compensatory evolution in fusidic acid-resistant Staphylococcus aureus. Mol Microbiol 40: 433-439.
    • (2001) Mol Microbiol , vol.40 , pp. 433-439
    • Nagaev, I.1    Bjorkman, J.2    Andersson, D.I.3    Hughes, D.4
  • 37
    • 0019851746 scopus 로고
    • Rearrangements in the chloroplast genome of mung bean and pea
    • Palmer JD, Thompson WF (1981) Rearrangements in the chloroplast genome of mung bean and pea. Proc Natl Acad Sci USA 78: 5533-5537.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 5533-5537
    • Palmer, J.D.1    Thompson, W.F.2
  • 40
    • 67650457908 scopus 로고    scopus 로고
    • Bacterial alarmone, guanosine 5′-diphosphate 3′-diphosphate (ppGpp), predominantly binds the β' subunit of plastid-encoded plastid RNA polymerase in chloroplasts
    • Sato M, Takahashi K, Ochiai Y, Hosaka T, Ochi K, Nabeta K (2009) Bacterial alarmone, guanosine 5′-diphosphate 3′-diphosphate (ppGpp), predominantly binds the β' subunit of plastid-encoded plastid RNA polymerase in chloroplasts. Chembiochem 10: 1227-1233.
    • (2009) Chembiochem , vol.10 , pp. 1227-1233
    • Sato, M.1    Takahashi, K.2    Ochiai, Y.3    Hosaka, T.4    Ochi, K.5    Nabeta, K.6
  • 42
    • 0022349250 scopus 로고
    • Euglena gracilis chloroplast elongation factor Tu. Interaction with guanine nucleotides and aminoacyl-tRNA
    • Sreedharan SP, Spremulli LL (1985) Euglena gracilis chloroplast elongation factor Tu. Interaction with guanine nucleotides and aminoacyl-tRNA. J Biol Chem 260: 8771-8776.
    • (1985) J Biol Chem , vol.260 , pp. 8771-8776
    • Sreedharan, S.P.1    Spremulli, L.L.2
  • 43
    • 42149158392 scopus 로고    scopus 로고
    • Control of bacterial transcription, translation and replication by (p)ppGpp
    • Srivatsan A, Wang JD (2008) Control of bacterial transcription, translation and replication by (p)ppGpp. Curr Opin Microbiol 11: 100-105.
    • (2008) Curr Opin Microbiol , vol.11 , pp. 100-105
    • Srivatsan, A.1    Wang, J.D.2
  • 44
    • 0030774006 scopus 로고    scopus 로고
    • Transcription and translation in chloroplasts
    • Stern DS, Higgs DC, Yang J (1997) Transcription and translation in chloroplasts. Trends Plant Sci 2: 308-315.
    • (1997) Trends Plant Sci , vol.2 , pp. 308-315
    • Stern, D.S.1    Higgs, D.C.2    Yang, J.3
  • 45
    • 0032411339 scopus 로고    scopus 로고
    • Evolution and mechanism of translation in chloroplasts
    • Sugiura M, Hirose T, Sugita M (1998) Evolution and mechanism of translation in chloroplasts. Annu Rev Genet 32: 437-459.
    • (1998) Annu Rev Genet , vol.32 , pp. 437-459
    • Sugiura, M.1    Hirose, T.2    Sugita, M.3
  • 46
    • 1642528990 scopus 로고    scopus 로고
    • Identification of the bacterial alarmone guanosine 5′-diphosphate 3′-diphosphate (ppGpp) in plants
    • Takahashi K, Kasai K, Ochi K (2004) Identification of the bacterial alarmone guanosine 5′-diphosphate 3′-diphosphate (ppGpp) in plants. Proc Natl Acad Sci U S A 101: 4320-4324.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4320-4324
    • Takahashi, K.1    Kasai, K.2    Ochi, K.3
  • 47
    • 79958763710 scopus 로고    scopus 로고
    • A central interdomain protein joint in elongation factor G regulates antibiotic sensitivity, GTP hydrolysis, and ribosome translocation
    • Ticu C, Murataliev M, Nechifor R, Wilson KS (2011) A central interdomain protein joint in elongation factor G regulates antibiotic sensitivity, GTP hydrolysis, and ribosome translocation. J Biol Chem 286: 21697-21705.
    • (2011) J Biol Chem , vol.286 , pp. 21697-21705
    • Ticu, C.1    Murataliev, M.2    Nechifor, R.3    Wilson, K.S.4
  • 48
    • 79961029191 scopus 로고    scopus 로고
    • Signalling by the global regulatory molecule ppGpp in bacteria and chloroplasts of land plants
    • Tozawa Y, Nomura Y (2011) Signalling by the global regulatory molecule ppGpp in bacteria and chloroplasts of land plants. Plant Biol (Stuttg) 13: 699-709.
    • (2011) Plant Biol (Stuttg) , vol.13 , pp. 699-709
    • Tozawa, Y.1    Nomura, Y.2
  • 50
    • 0027137079 scopus 로고
    • Cloning and nucleotide sequence of a tobacco chloroplast translational elongation factor, EF-Tu
    • Ursin VM, Becker CK, Shewmaker CK (1993) Cloning and nucleotide sequence of a tobacco chloroplast translational elongation factor, EF-Tu. Plant Physiol 101: 333-334.
    • (1993) Plant Physiol , vol.101 , pp. 333-334
    • Ursin, V.M.1    Becker, C.K.2    Shewmaker, C.K.3
  • 52
    • 0034665988 scopus 로고    scopus 로고
    • The plastid ribosomal proteins. Identification of all the proteins in the 50 S subunit of an organelle ribosome (chloroplast)
    • Yamaguchi K, Subramanian AR (2000) The plastid ribosomal proteins. Identification of all the proteins in the 50 S subunit of an organelle ribosome (chloroplast). J Biol Chem 275: 28466-28482.
    • (2000) J Biol Chem , vol.275 , pp. 28466-28482
    • Yamaguchi, K.1    Subramanian, A.R.2
  • 53
    • 0034666124 scopus 로고    scopus 로고
    • The plastid ribosomal proteins. Identification of all the proteins in the 30 S subunit of an organelle ribosome (chloroplast)
    • Yamaguchi K, von Knoblauch K, Subramanian AR (2000) The plastid ribosomal proteins. Identification of all the proteins in the 30 S subunit of an organelle ribosome (chloroplast). J Biol Chem 275: 28455-28465.
    • (2000) J Biol Chem , vol.275 , pp. 28455-28465
    • Yamaguchi, K.1    von Knoblauch, K.2    Subramanian, A.R.3
  • 54
    • 0015509127 scopus 로고
    • Inhibition of translation initiation complex formation by MS1
    • Yoshida M, Travers A, Clark BF (1972) Inhibition of translation initiation complex formation by MS1. FEBS Lett 23: 163-166.
    • (1972) FEBS Lett , vol.23 , pp. 163-166
    • Yoshida, M.1    Travers, A.2    Clark, B.F.3
  • 55
    • 33846065241 scopus 로고    scopus 로고
    • A new in vitro translation system for non-radioactive assay from tobacco chloroplasts: effect of pre-mRNA processing on translation in vitro
    • Yukawa M, Kuroda H, Sugiura M (2007) A new in vitro translation system for non-radioactive assay from tobacco chloroplasts: effect of pre-mRNA processing on translation in vitro. Plant J 49: 367-376.
    • (2007) Plant J , vol.49 , pp. 367-376
    • Yukawa, M.1    Kuroda, H.2    Sugiura, M.3
  • 56
    • 0033851987 scopus 로고    scopus 로고
    • Translation in chloroplasts
    • Zerges W (2000) Translation in chloroplasts. Biochimie 82: 583-601.
    • (2000) Biochimie , vol.82 , pp. 583-601
    • Zerges, W.1


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