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Volumn 176, Issue 5, 2009, Pages 635-642

Molecular characterization of a biotic and abiotic stress resistance-related gene RelA/SpoT homologue (PepRSH) from pepper

Author keywords

(p)ppGpp synthetase; Biotic and abiotic stress; Pepper

Indexed keywords

BACTERIA (MICROORGANISMS); CAPSICUM FRUTESCENS; ESCHERICHIA COLI;

EID: 61849151869     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2009.02.004     Document Type: Article
Times cited : (21)

References (29)
  • 1
    • 0003174053 scopus 로고    scopus 로고
    • The stringent response
    • Neidhartt F.C., Ingraham J.C., Brooks L.K., Magasanik B., Schaechter M., and Umbarger H.E. (Eds), American Society for microbiology Press, Washington DC
    • Cashel M., Gentry D.R., Hernadez V.J., and Vinella D. The stringent response. In: Neidhartt F.C., Ingraham J.C., Brooks L.K., Magasanik B., Schaechter M., and Umbarger H.E. (Eds). Escherichia coli and Salmonella typhimurium: cellular and molecular biology (1996), American Society for microbiology Press, Washington DC 1458-1496
    • (1996) Escherichia coli and Salmonella typhimurium: cellular and molecular biology , pp. 1458-1496
    • Cashel, M.1    Gentry, D.R.2    Hernadez, V.J.3    Vinella, D.4
  • 3
    • 0029985489 scopus 로고    scopus 로고
    • Mutational analysis of the Escherichia coli spoT gene identifies distinct but overlapping regions involved in ppGpp synthesis and degradation
    • Gentry D.R., and Cashel M. Mutational analysis of the Escherichia coli spoT gene identifies distinct but overlapping regions involved in ppGpp synthesis and degradation. Mol. Microbiol. 19 (1996) 1373-1384
    • (1996) Mol. Microbiol. , vol.19 , pp. 1373-1384
    • Gentry, D.R.1    Cashel, M.2
  • 4
    • 0034866076 scopus 로고    scopus 로고
    • Comparative genomics and evolution of genes encoding bacterial (p)ppGpp synthetases/hydrolases (the Rel, RelA and SpoT proteins)
    • Mittenhuber G. Comparative genomics and evolution of genes encoding bacterial (p)ppGpp synthetases/hydrolases (the Rel, RelA and SpoT proteins). J. Mol. Microbiol. Biotechnol. 3 (2001) 585-600
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 585-600
    • Mittenhuber, G.1
  • 6
    • 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 R.M., Lin M.H., Taylor D.J., Mechold U., Berry J.O., and Hernandez V.J. Inducible expression, enzymatic activity, and origin of higher plant homologues of bacterial RelA/SpoT stress proteins in Nicotiana tabacum. J. Biol. Chem. 279 (2004) 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
  • 7
    • 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., and Tozawa Y. 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 (2002) 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
  • 8
    • 0037267572 scopus 로고    scopus 로고
    • Plant RelA/SpoT homolog confers salt tolerance in Escherichia coli and Saccharomyces cerevisiae
    • Yamada A., Tsutsumi K., Tanimoto S., and Ozeki Y. Plant RelA/SpoT homolog confers salt tolerance in Escherichia coli and Saccharomyces cerevisiae. Plant Cell Physiol. 44 (2003) 3-9
    • (2003) Plant Cell Physiol. , vol.44 , pp. 3-9
    • Yamada, A.1    Tsutsumi, K.2    Tanimoto, S.3    Ozeki, Y.4
  • 9
    • 1642528990 scopus 로고    scopus 로고
    • Identification of the bacterial alarmone guanosine 5′-diphosphate 3′-diphosphate (ppGpp) in plants
    • Takahashi K., Kasai K., and Ochi K. Identification of the bacterial alarmone guanosine 5′-diphosphate 3′-diphosphate (ppGpp) in plants. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 4320-4324
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 4320-4324
    • Takahashi, K.1    Kasai, K.2    Ochi, K.3
  • 10
    • 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., and Tozawa Y. Guanosine tetra- and pentaphosphate synthase activity in chloroplasts of a higher plant: association with 70S ribosomes and inhibition by tetracycline. Nucleic Acids Res. 32 (2004) 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
  • 11
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O., Nielsen H., Brunak S., and von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 300 (2000) 1005-1016
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    von Heijne, G.4
  • 12
    • 0032935861 scopus 로고    scopus 로고
    • ChloroP, a neural network-based method for predicting chloroplast transient peptides and their cleavage sites
    • Emanuelsson O., Nielsen H., and von Heijne G. ChloroP, a neural network-based method for predicting chloroplast transient peptides and their cleavage sites. Protein Sci. 8 (1999) 978-984
    • (1999) Protein Sci. , vol.8 , pp. 978-984
    • Emanuelsson, O.1    Nielsen, H.2    von Heijne, G.3
  • 13
    • 0027105007 scopus 로고
    • A knowledge base for predicting protein localization sites in eukaryotic cells
    • Nakai K., and Kanehisa M. A knowledge base for predicting protein localization sites in eukaryotic cells. Genomics 14 (1992) 897-911
    • (1992) Genomics , vol.14 , pp. 897-911
    • Nakai, K.1    Kanehisa, M.2
  • 14
    • 0025992789 scopus 로고
    • Residual guanosine 3′,5′-bipyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations
    • Xiao H., Kalman M., Ikehara K., Zemel S., Glaser G., and Cashel M. Residual guanosine 3′,5′-bipyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations. J. Biol. Chem. 266 (1991) 5980-5990
    • (1991) J. Biol. Chem. , vol.266 , pp. 5980-5990
    • Xiao, H.1    Kalman, M.2    Ikehara, K.3    Zemel, S.4    Glaser, G.5    Cashel, M.6
  • 15
    • 0032408864 scopus 로고    scopus 로고
    • The HD domain defines a new superfamily of metal-dependent phosphohydrolases
    • Aravind L., and Koonin E. The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Trends Biol. Sci. 23 (1998) 469-472
    • (1998) Trends Biol. Sci. , vol.23 , pp. 469-472
    • Aravind, L.1    Koonin, E.2
  • 16
    • 0027756183 scopus 로고
    • Active oxygen species in the induction of plant systemic acquired resistance by salicylic acid
    • Chen Z., Silva H., and Klessig D.F. Active oxygen species in the induction of plant systemic acquired resistance by salicylic acid. Science 17 (1993) 1883-1886
    • (1993) Science , vol.17 , pp. 1883-1886
    • Chen, Z.1    Silva, H.2    Klessig, D.F.3
  • 17
    • 0029170012 scopus 로고
    • UV-B induced PR-1 accumulation is mediated by active oxygen species
    • Green R., and Fluhr R. UV-B induced PR-1 accumulation is mediated by active oxygen species. Plant Cell 7 (1995) 203-212
    • (1995) Plant Cell , vol.7 , pp. 203-212
    • Green, R.1    Fluhr, R.2
  • 18
    • 0017106681 scopus 로고
    • A rapid test for the RelA mutation in E. coli
    • Uzan M., and Danchin A. A rapid test for the RelA mutation in E. coli. Biochem. Biophys. Res. Commun. 69 (1976) 751-758
    • (1976) Biochem. Biophys. Res. Commun. , vol.69 , pp. 751-758
    • Uzan, M.1    Danchin, A.2
  • 19
    • 0026788401 scopus 로고
    • Toxic effects of high levels of ppGpp in Escherichia coli are relieved by rpoB mutations
    • Tedin K., and Bremer H. Toxic effects of high levels of ppGpp in Escherichia coli are relieved by rpoB mutations. J. Biol. Chem. 267 (1992) 2337-2344
    • (1992) J. Biol. Chem. , vol.267 , pp. 2337-2344
    • Tedin, K.1    Bremer, H.2
  • 20
    • 0035075387 scopus 로고    scopus 로고
    • Revisiting the stringent response, ppGpp and starvation signaling
    • Chatterji D., and Ojha A.K. Revisiting the stringent response, ppGpp and starvation signaling. Curr. Opin. Microbiol. 4 (2001) 160-165
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 160-165
    • Chatterji, D.1    Ojha, A.K.2
  • 21
    • 0034686043 scopus 로고    scopus 로고
    • RpoS-dependent promoter require guanosine tetraphosphate for induction even in the presence of high levels of δs
    • Kvint K., Farewell A., and Nyström T. RpoS-dependent promoter require guanosine tetraphosphate for induction even in the presence of high levels of δs. J. Biol. Chem. 275 (2000) 14795-14798
    • (2000) J. Biol. Chem. , vol.275 , pp. 14795-14798
    • Kvint, K.1    Farewell, A.2    Nyström, T.3
  • 22
    • 0036192462 scopus 로고    scopus 로고
    • The universal stress protein paralogues of Escherichia coli are coordinarily regulated and cooperate in the defense against DNA damage
    • Gustavsson N., Diez A., and Nyström T. The universal stress protein paralogues of Escherichia coli are coordinarily regulated and cooperate in the defense against DNA damage. Mol. Microbiol. 43 (2002) 107-117
    • (2002) Mol. Microbiol. , vol.43 , pp. 107-117
    • Gustavsson, N.1    Diez, A.2    Nyström, T.3
  • 23
    • 0037093379 scopus 로고    scopus 로고
    • Regulation of sigma factor competition by the alarmone ppGpp
    • Jishage M., Kvint K., Shingler V., and Nystro{combining double acute accent}m T. Regulation of sigma factor competition by the alarmone ppGpp. Genes Dev. 16 (2002) 1260-1270
    • (2002) Genes Dev. , vol.16 , pp. 1260-1270
    • Jishage, M.1    Kvint, K.2    Shingler, V.3    Nystrom, T.4
  • 24
    • 0017986804 scopus 로고
    • The suppression of defective translation by ppGpp and its role in stringent response
    • O'Farrel P.H. The suppression of defective translation by ppGpp and its role in stringent response. Cell 14 (1978) 545-557
    • (1978) Cell , vol.14 , pp. 545-557
    • O'Farrel, P.H.1
  • 26
    • 0034682529 scopus 로고    scopus 로고
    • Enhancement of induced disease resistance by simultaneous activation of salicylate- and jasmonate-dependent defense pathways in Arabidopsis thaliana
    • van Wees S.C.M., de Swart E.A.M., vanPelt J.A., van Loon L.C., and Pieterse C.M.J. Enhancement of induced disease resistance by simultaneous activation of salicylate- and jasmonate-dependent defense pathways in Arabidopsis thaliana. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 8711-8716
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8711-8716
    • van Wees, S.C.M.1    de Swart, E.A.M.2    vanPelt, J.A.3    van Loon, L.C.4    Pieterse, C.M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.