메뉴 건너뛰기




Volumn 53, Issue 5, 2007, Pages 551-558

Cold-stress-altered phosphorylation of EF-Tu in the cyanobacterium Anabaena sp. strain PCC 7120

Author keywords

Cold stress; EF TU phosphorylation; Ribosomal protein S2; Threonine kinase

Indexed keywords

ACCLIMATION PHASE; PROKARYOTES; RIBOSOME; THREONINE KINASE;

EID: 34547762127     PISSN: 00084166     EISSN: None     Source Type: Journal    
DOI: 10.1139/W07-030     Document Type: Article
Times cited : (6)

References (39)
  • 1
    • 0035794713 scopus 로고    scopus 로고
    • Molecular basis of thermosensing: A two-component signal transduction thermometer in Bacillus subtilis
    • doi:10.1093/emboj/20.7.1681
    • Aguilar, P.S., Hernandez-Arriaga, A.M., Cybulski, L.E., Erazo, A.C., and de Mendoza, D. 2001. Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis. EMBO J. 20: 1681-1691. doi:10.1093/emboj/20.7.1681.
    • (2001) EMBO J , vol.20 , pp. 1681-1691
    • Aguilar, P.S.1    Hernandez-Arriaga, A.M.2    Cybulski, L.E.3    Erazo, A.C.4    de Mendoza, D.5
  • 3
    • 0024617891 scopus 로고
    • Salinity-stress-induced proteins in two nitrogen-fixing Anabaena strains differentially tolerant to salt
    • Apte, S.K., and Bhagwat, A.A. 1989. Salinity-stress-induced proteins in two nitrogen-fixing Anabaena strains differentially tolerant to salt. J. Bacteriol. 171: 909-915.
    • (1989) J. Bacteriol , vol.171 , pp. 909-915
    • Apte, S.K.1    Bhagwat, A.A.2
  • 4
    • 0028057181 scopus 로고
    • Ribosomal protein S2/Sa kinase purified from HeLa cells infected with vaccinia virus corresponds to the B1R protein kinase and phosphorylates in vitro the viral ssDNA-binding protein
    • Beaud, G., Sharif, A., Topa-Massé, A., and Leader, D.P. 1994. Ribosomal protein S2/Sa kinase purified from HeLa cells infected with vaccinia virus corresponds to the B1R protein kinase and phosphorylates in vitro the viral ssDNA-binding protein. J. Gen. Virol. 75: 283-293.
    • (1994) J. Gen. Virol , vol.75 , pp. 283-293
    • Beaud, G.1    Sharif, A.2    Topa-Massé, A.3    Leader, D.P.4
  • 5
    • 0023133375 scopus 로고
    • Ribosomal protein phosphorylation in vivo and in vitro by vaccinia virus
    • doi:10.1111/j.1432-1033.1987.tb10547.x
    • Buendia, B., Person-Fernandez, A., Beaud, G., and Madjar, J.-J. 1987. Ribosomal protein phosphorylation in vivo and in vitro by vaccinia virus. Eur. J. Biochem. 162: 95-103. doi:10.1111/j.1432-1033.1987.tb10547.x.
    • (1987) Eur. J. Biochem , vol.162 , pp. 95-103
    • Buendia, B.1    Person-Fernandez, A.2    Beaud, G.3    Madjar, J.-J.4
  • 6
    • 0033983750 scopus 로고    scopus 로고
    • Regulation of cold shock-induced RNA helicase gene expression in the cyanobacterium Anabaena sp. strain PCC 7120
    • doi:10.1128/JB.182.5.1251-1256.2000
    • Chamot, D., and Owttrim, G.W. 2000. Regulation of cold shock-induced RNA helicase gene expression in the cyanobacterium Anabaena sp. strain PCC 7120. J. Bacteriol. 182: 1251-1256. doi:10.1128/JB.182.5.1251-1256.2000.
    • (2000) J. Bacteriol , vol.182 , pp. 1251-1256
    • Chamot, D.1    Owttrim, G.W.2
  • 7
    • 0032992366 scopus 로고    scopus 로고
    • A cold shock-induced cyanobacterial RNA helicase
    • Chamot, D., Magee, W.C., Yu, E., and Owttrim, G.W. 1999. A cold shock-induced cyanobacterial RNA helicase. J. Bacteriol. 181: 1728-1732.
    • (1999) J. Bacteriol , vol.181 , pp. 1728-1732
    • Chamot, D.1    Magee, W.C.2    Yu, E.3    Owttrim, G.W.4
  • 8
    • 0028036559 scopus 로고
    • Control of translation by mRNA secondary structure in Escherichia coli. A quantitative analysis of literature data
    • doi:10.1006/jmbi.1994.1714
    • de Smit, M.H., and van Duin, J. 1994. Control of translation by mRNA secondary structure in Escherichia coli. A quantitative analysis of literature data. J. Mol. Biol. 244: 144-150. doi:10.1006/jmbi.1994.1714.
    • (1994) J. Mol. Biol , vol.244 , pp. 144-150
    • de Smit, M.H.1    van Duin, J.2
  • 9
    • 0036867143 scopus 로고    scopus 로고
    • Bacterial cold-shock proteins
    • doi:10.1007/PL00012513
    • Ermolenko, D.N., and Makhatadze, G.I. 2002. Bacterial cold-shock proteins. Cell. Mol. Life Sci. 59: 1902-1913. doi:10.1007/PL00012513.
    • (2002) Cell. Mol. Life Sci , vol.59 , pp. 1902-1913
    • Ermolenko, D.N.1    Makhatadze, G.I.2
  • 10
    • 0031023549 scopus 로고    scopus 로고
    • Promoter-independent cold-shock induction of cspA and its derepression at 37 °C by mRNA stabilization
    • doi:10.1046/j.1365-2958.1997. 2351592.x
    • Fang, L., Jiang, W., Bae, W., and Inouye, M. 1997. Promoter-independent cold-shock induction of cspA and its derepression at 37 °C by mRNA stabilization. Mol. Microbiol. 23: 355-364. doi:10.1046/j.1365-2958.1997. 2351592.x.
    • (1997) Mol. Microbiol , vol.23 , pp. 355-364
    • Fang, L.1    Jiang, W.2    Bae, W.3    Inouye, M.4
  • 11
    • 1642580810 scopus 로고    scopus 로고
    • Preferential translation of cold-shock mRNAs during cold adaptation
    • doi:10.1261/rna.5164904
    • Giuliodori, A.M., Brandi, M.A., Gualerzi, C.O., and Pon, C.L. 2004. Preferential translation of cold-shock mRNAs during cold adaptation. RNA, 10: 265-276. doi:10.1261/rna.5164904.
    • (2004) RNA , vol.10 , pp. 265-276
    • Giuliodori, A.M.1    Brandi, M.A.2    Gualerzi, C.O.3    Pon, C.L.4
  • 12
    • 0029823884 scopus 로고    scopus 로고
    • Some like it cold: Response of microorganisms to cold shock
    • doi:10.1007/s002030050386
    • Graumann, P., and Marahiel, M.A. 1996. Some like it cold: response of microorganisms to cold shock. Arch. Microbiol. 166: 293-300. doi:10.1007/s002030050386.
    • (1996) Arch. Microbiol , vol.166 , pp. 293-300
    • Graumann, P.1    Marahiel, M.A.2
  • 13
    • 0043166304 scopus 로고    scopus 로고
    • Transcriptional and post-transcriptional control of cold-shock genes
    • doi:10.1016/S0022-2836(03)00732-0
    • Gualerzi, C.O., Giuliodori, A.M., and Pon, C.L. 2003. Transcriptional and post-transcriptional control of cold-shock genes. J. Mol. Biol. 331: 527-539. doi:10.1016/S0022-2836(03)00732-0.
    • (2003) J. Mol. Biol , vol.331 , pp. 527-539
    • Gualerzi, C.O.1    Giuliodori, A.M.2    Pon, C.L.3
  • 14
    • 0027459168 scopus 로고
    • Effects of protein kinase inhibitors on in vitro protein phosphorylation and cellular differentiation of Streptomyces griseus
    • doi:10.1007/BF00277132
    • Hong, S.K., Matsumoto, A., Horinouchi, S., and Beppu, T. 1993. Effects of protein kinase inhibitors on in vitro protein phosphorylation and cellular differentiation of Streptomyces griseus. Mol. Gen. Genet. 236: 347-354. doi:10.1007/BF00277132.
    • (1993) Mol. Gen. Genet , vol.236 , pp. 347-354
    • Hong, S.K.1    Matsumoto, A.2    Horinouchi, S.3    Beppu, T.4
  • 16
    • 0021983259 scopus 로고
    • Phosphorylation-dephosphorylation changes in yeast ribosomal proteins S2 and S6 during growth under normal and hyperthermal conditions
    • Jakubowicz, T. 1985. Phosphorylation-dephosphorylation changes in yeast ribosomal proteins S2 and S6 during growth under normal and hyperthermal conditions. Acta Biochim. Pol. 32: 7-12.
    • (1985) Acta Biochim. Pol , vol.32 , pp. 7-12
    • Jakubowicz, T.1
  • 17
    • 0028363836 scopus 로고
    • The cold-shock response - a hot topic
    • doi:10.1111/j.1365-2958.1994.tb00359.x
    • Jones, P.G., and Inouye, M. 1994. The cold-shock response - a hot topic. Mol. Microbiol. 11: 811-818. doi:10.1111/j.1365-2958.1994.tb00359.x.
    • (1994) Mol. Microbiol , vol.11 , pp. 811-818
    • Jones, P.G.1    Inouye, M.2
  • 18
    • 0029786252 scopus 로고    scopus 로고
    • RbfA, a 30S ribosomal binding factor, is a cold-shock protein whose absence triggers the cold-shock response
    • doi:10.1111/j.1365-2958.1996.tb02582.x
    • Jones, P.G., and Inouye, M. 1996. RbfA, a 30S ribosomal binding factor, is a cold-shock protein whose absence triggers the cold-shock response. Mol. Microbiol. 21: 1207-1218. doi:10.1111/j.1365-2958.1996.tb02582.x.
    • (1996) Mol. Microbiol , vol.21 , pp. 1207-1218
    • Jones, P.G.1    Inouye, M.2
  • 19
    • 0030043216 scopus 로고    scopus 로고
    • Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli
    • doi:10.1073/pnas.93.1.76
    • Jones, P.G., Mitta, M., Kim, Y., Jiang, W., and Inouye, M. 1996. Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 93: 76-80. doi:10.1073/pnas.93.1.76.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 76-80
    • Jones, P.G.1    Mitta, M.2    Kim, Y.3    Jiang, W.4    Inouye, M.5
  • 20
    • 0033258542 scopus 로고    scopus 로고
    • Translational regulation by modifications of the elongation factor Tu
    • Kraal, B., Lippmann, C., and Kleanthous, C. 1999. Translational regulation by modifications of the elongation factor Tu. Folia Microbiol. (Praha), 44: 131-141.
    • (1999) Folia Microbiol. (Praha) , vol.44 , pp. 131-141
    • Kraal, B.1    Lippmann, C.2    Kleanthous, C.3
  • 21
    • 0035958678 scopus 로고    scopus 로고
    • Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli
    • doi:10.1126/science.1061315
    • Kuroda, A., Nomura, K, Ohtomo, R., Kato, J., Ikeda, T., Takiguchi, N., Ohtake, H., and Romberg, A. 2001. Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli. Science (Washington, D.C.), 293: 705-708. doi:10.1126/science.1061315.
    • (2001) Science (Washington, D.C.) , vol.293 , pp. 705-708
    • Kuroda, A.1    Nomura, K.2    Ohtomo, R.3    Kato, J.4    Ikeda, T.5    Takiguchi, N.6    Ohtake, H.7    Romberg, A.8
  • 22
    • 0036433494 scopus 로고    scopus 로고
    • The histidine kinase Hik33 perceives osmotic stress and cold stress in Synechocystis sp. PCC 6803
    • doi:10.1046/j.1365-2958.2002. 03202.x
    • Mikami, K, Kanesaki, Y., Suzuki, I., and Murata, N. 2002. The histidine kinase Hik33 perceives osmotic stress and cold stress in Synechocystis sp. PCC 6803. Mol. Microbiol. 46: 905-915. doi:10.1046/j.1365-2958.2002. 03202.x.
    • (2002) Mol. Microbiol , vol.46 , pp. 905-915
    • Mikami, K.1    Kanesaki, Y.2    Suzuki, I.3    Murata, N.4
  • 23
    • 0029148050 scopus 로고
    • Sequencing of the tuf1 gene and the phosphorylation pattern of EF-Tu1 during development and differentiation in Streptomyces collinus producing kirromycin
    • doi:10.1006/bbrc.1995.2153
    • Mikulik, K., and Zhulanova, E. 1995. Sequencing of the tuf1 gene and the phosphorylation pattern of EF-Tu1 during development and differentiation in Streptomyces collinus producing kirromycin. Biochem. Biophys. Res. Commun. 213: 454-461. doi:10.1006/bbrc.1995.2153.
    • (1995) Biochem. Biophys. Res. Commun , vol.213 , pp. 454-461
    • Mikulik, K.1    Zhulanova, E.2
  • 24
    • 0036015651 scopus 로고    scopus 로고
    • Effects of ribosomal proteins S1, S2 and the DeaD/CsdA DEAD-box helicase on translation of leaderless and canonical mRNAs in Escherichia coli
    • doi:10.1046/j.1365-2958.2002.02971.x
    • Moll, I., Grill, S., Gründling, A., and Bläsi, U. 2002. Effects of ribosomal proteins S1, S2 and the DeaD/CsdA DEAD-box helicase on translation of leaderless and canonical mRNAs in Escherichia coli. Mol. Microbiol. 44: 1387-1396. doi:10.1046/j.1365-2958.2002.02971.x.
    • (2002) Mol. Microbiol , vol.44 , pp. 1387-1396
    • Moll, I.1    Grill, S.2    Gründling, A.3    Bläsi, U.4
  • 25
    • 0022442610 scopus 로고
    • Purification and characterization of phosphoenolpyruvate carboxylase from a cyanobacterium
    • Owttrim, G.W., and Colman, B. 1986. Purification and characterization of phosphoenolpyruvate carboxylase from a cyanobacterium. J. Bacteriol. 168: 207-212.
    • (1986) J. Bacteriol , vol.168 , pp. 207-212
    • Owttrim, G.W.1    Colman, B.2
  • 26
    • 1942467448 scopus 로고    scopus 로고
    • Recent developments in bacterial cold-shock response
    • Phadtare, S. 2004. Recent developments in bacterial cold-shock response. Curr. Issues Mol. Biol. 6: 125-136.
    • (2004) Curr. Issues Mol. Biol , vol.6 , pp. 125-136
    • Phadtare, S.1
  • 27
    • 0032563095 scopus 로고    scopus 로고
    • Ribosomal protein S1 is required for translation of most, if not all, natural mRNAs in Escherichia coli in vivo
    • doi:10.1006/jmbi.1998.1909
    • Sørensen, M.A., Fricke, J., and Pedersen, S. 1998. Ribosomal protein S1 is required for translation of most, if not all, natural mRNAs in Escherichia coli in vivo. J. Mol. Biol. 280: 561-569. doi:10.1006/jmbi.1998.1909.
    • (1998) J. Mol. Biol , vol.280 , pp. 561-569
    • Sørensen, M.A.1    Fricke, J.2    Pedersen, S.3
  • 28
    • 21344466112 scopus 로고    scopus 로고
    • Identification and regulation of cold-inducible factors of Bordetella bonchiseptica
    • doi:10.1099/mic.0.27785-0
    • Stübs, D., Fuchs, T.M., Schneider, B., Bosserhoff, A., and Gross, R. 2005. Identification and regulation of cold-inducible factors of Bordetella bonchiseptica. Microbiology (Reading, U.K.), 151: 1895-1909. doi:10.1099/mic.0.27785-0.
    • (2005) Microbiology (Reading, U.K.) , vol.151 , pp. 1895-1909
    • Stübs, D.1    Fuchs, T.M.2    Schneider, B.3    Bosserhoff, A.4    Gross, R.5
  • 29
    • 0342546000 scopus 로고    scopus 로고
    • The pathway for perception and transduction of low-temperature signals in Synechocystis
    • doi:10.1093/emboj/19.6.1327
    • Suzuki, I., Los, D.A., Kanesaki, Y., Mikami, K., and Murata, N. 2000. The pathway for perception and transduction of low-temperature signals in Synechocystis. EMBO J. 19: 1327-1334. doi:10.1093/emboj/19.6.1327.
    • (2000) EMBO J , vol.19 , pp. 1327-1334
    • Suzuki, I.1    Los, D.A.2    Kanesaki, Y.3    Mikami, K.4    Murata, N.5
  • 30
    • 0030875652 scopus 로고    scopus 로고
    • Requirements for ribosomal protein S1 for translation initiation of mRNAs with and without a 5′ leader sequence
    • doi:10.1046/j.1365-2958. 1997.4421810.x
    • Tedin, K., Resch, A., and Bläsi, U. 1997. Requirements for ribosomal protein S1 for translation initiation of mRNAs with and without a 5′ leader sequence. Mol. Microbiol. 25: 189-199. doi:10.1046/j.1365-2958. 1997.4421810.x.
    • (1997) Mol. Microbiol , vol.25 , pp. 189-199
    • Tedin, K.1    Resch, A.2    Bläsi, U.3
  • 31
    • 0025733344 scopus 로고
    • deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RNA helicase, can suppress a mutation in rpsB, the gene encoding ribosomal protein S2
    • Toone, W.M., Rudd, K.E., and Friesen, J.D. 1991. deaD, a new Escherichia coli gene encoding a presumed ATP-dependent RNA helicase, can suppress a mutation in rpsB, the gene encoding ribosomal protein S2. J. Bacteriol. 173: 3291-3302.
    • (1991) J. Bacteriol , vol.173 , pp. 3291-3302
    • Toone, W.M.1    Rudd, K.E.2    Friesen, J.D.3
  • 32
    • 0016733030 scopus 로고
    • Function of Escherichia coli ribosomal protein S1 in translation of natural and synthetic messenger RNA
    • van Dieijen, G., van der Laken, C.J., van Knippenberg, P.H., and van Duin, J. 1975. Function of Escherichia coli ribosomal protein S1 in translation of natural and synthetic messenger RNA. J. Mol. Biol. 93: 351-366.
    • (1975) J. Mol. Biol , vol.93 , pp. 351-366
    • van Dieijen, G.1    van der Laken, C.J.2    van Knippenberg, P.H.3    van Duin, J.4
  • 33
    • 0037126659 scopus 로고    scopus 로고
    • Genomic analysis of protein kinases, protein phosphatases and two-component regulatory systems of the cyanobacterium Anabaena sp. strain PCC 7120
    • doi:10.1111/j.1574-6968.2002.tb11469. x
    • Wang, L., Sun, Y.-P., Chen, W.-L., Li, J.-H., and Zhang, C.-C. 2002. Genomic analysis of protein kinases, protein phosphatases and two-component regulatory systems of the cyanobacterium Anabaena sp. strain PCC 7120. FEMS Microbiol. Lett. 217: 155-165. doi:10.1111/j.1574-6968.2002.tb11469. x.
    • (2002) FEMS Microbiol. Lett , vol.217 , pp. 155-165
    • Wang, L.1    Sun, Y.-P.2    Chen, W.-L.3    Li, J.-H.4    Zhang, C.-C.5
  • 34
    • 0041909570 scopus 로고    scopus 로고
    • Bacterial cold shock responses
    • Weber, M.H., and Marahiel, M.A. 2003. Bacterial cold shock responses. Sci. Prog. 86: 9-75.
    • (2003) Sci. Prog , vol.86 , pp. 9-75
    • Weber, M.H.1    Marahiel, M.A.2
  • 35
    • 0033546122 scopus 로고    scopus 로고
    • High-throughput mass spectrometric discovery of protein post-translational modifications
    • doi:10.1006/jmbi.1999.2794
    • Wilkins, M.R., Gasteiger, E., Gooley, A.A., Herbert, B.R., Molloy, M.P., Binz, P.-A., et al. 1999. High-throughput mass spectrometric discovery of protein post-translational modifications. J. Mol. Biol. 289: 645-657. doi:10.1006/jmbi.1999.2794.
    • (1999) J. Mol. Biol , vol.289 , pp. 645-657
    • Wilkins, M.R.1    Gasteiger, E.2    Gooley, A.A.3    Herbert, B.R.4    Molloy, M.P.5    Binz, P.-A.6
  • 36
    • 0042510617 scopus 로고    scopus 로고
    • Regulated phosphorylation of 40S ribosomal protein S6 in root tips of maize
    • doi:10.1104/pp.103.022749
    • Williams, A.J., Werner-Fraczek, J., Chang, I.-F., and Bailey-Serres, J. 2003. Regulated phosphorylation of 40S ribosomal protein S6 in root tips of maize. Plant Physiol. 132: 2086-2097. doi:10.1104/pp.103.022749.
    • (2003) Plant Physiol , vol.132 , pp. 2086-2097
    • Williams, A.J.1    Werner-Fraczek, J.2    Chang, I.-F.3    Bailey-Serres, J.4
  • 37
    • 0034667906 scopus 로고    scopus 로고
    • Characterization of the cold stress-induced cyanobacterial DEAD-box protein CrhC as an RNA helicase
    • doi:10.1093/nar/28.20.3926
    • Yu, E., and Owttrim, G.W. 2000. Characterization of the cold stress-induced cyanobacterial DEAD-box protein CrhC as an RNA helicase. Nucleic Acids Res. 28: 3926-3934. doi:10.1093/nar/28.20.3926.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3926-3934
    • Yu, E.1    Owttrim, G.W.2
  • 38
    • 0032529472 scopus 로고    scopus 로고
    • Survey, analysis and genetic organization of genes encoding eukaryotic-like signaling proteins on a cyanobacterial genome
    • doi:10.1093/nar/26.16.3619
    • Zhang, C.-C., Gonzalez, L., and Phalip, V. 1998. Survey, analysis and genetic organization of genes encoding eukaryotic-like signaling proteins on a cyanobacterial genome. Nucleic Acids Res. 26: 3619-3625. doi:10.1093/nar/26.16.3619.
    • (1998) Nucleic Acids Res , vol.26 , pp. 3619-3625
    • Zhang, C.-C.1    Gonzalez, L.2    Phalip, V.3
  • 39
    • 30744463252 scopus 로고    scopus 로고
    • Protein phosphorylation on Ser, Thr, and Tyr residues in cyanobacteria
    • doi:10.1159/000089644
    • Zhang, C.-C., Jang, J., Sakr, S., and Wang, L. 2005. Protein phosphorylation on Ser, Thr, and Tyr residues in cyanobacteria. J. Mol. Microbiol. Biotechnol. 9: 154-166. doi:10.1159/000089644.
    • (2005) J. Mol. Microbiol. Biotechnol , vol.9 , pp. 154-166
    • Zhang, C.-C.1    Jang, J.2    Sakr, S.3    Wang, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.