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Volumn 360, Issue 1, 2007, Pages 209-217

Chlorella viruses contain genes encoding a complete polyamine biosynthetic pathway

Author keywords

Agmatine iminohydrolase; Arginine decarboxylase; Chlorella viruses; N Carbamoylputrescine amidohydrolase; PBCV 1; Phycodnaviridae; Polyamines

Indexed keywords

AGMATINE; AMIDASE; ARGININE; ARGININE DECARBOXYLASE; GENE PRODUCT; HYDROLASE; N CARBAMOYLPUTRESCINE; ORNITHINE DECARBOXYLASE; POLYAMINE; PROTEIN AIH; PUTRESCINE; PUTRESCINE DERIVATIVE; SPERMIDINE SYNTHASE; UNCLASSIFIED DRUG;

EID: 33847292966     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2006.10.010     Document Type: Article
Times cited : (35)

References (46)
  • 2
    • 0001457369 scopus 로고
    • The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid
    • Ames B.N., and Dubin D.T. The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J. Biol. Chem. 235 (1960) 769-775
    • (1960) J. Biol. Chem. , vol.235 , pp. 769-775
    • Ames, B.N.1    Dubin, D.T.2
  • 4
    • 26244460738 scopus 로고    scopus 로고
    • Isolation and characterization of a new type of chlorovirus that infects an endosymbiotic Chlorella strain of the heliozoon Acanthocystis turfacea
    • Bubeck J.A., and Pfitzner A.J. Isolation and characterization of a new type of chlorovirus that infects an endosymbiotic Chlorella strain of the heliozoon Acanthocystis turfacea. J. Gen. Virol. 86 (2005) 2871-2877
    • (2005) J. Gen. Virol. , vol.86 , pp. 2871-2877
    • Bubeck, J.A.1    Pfitzner, A.J.2
  • 6
    • 33847269821 scopus 로고    scopus 로고
    • Viruses
    • Oxford Univ. Press Inc., New York
    • Cohen S.S. Viruses. A Guide to the Polyamines (1998), Oxford Univ. Press Inc., New York 366-395
    • (1998) A Guide to the Polyamines , pp. 366-395
    • Cohen, S.S.1
  • 7
    • 0018654297 scopus 로고
    • Polyamines and virus multiplication
    • Cohen S.S., and McCormick F.P. Polyamines and virus multiplication. Adv. Virus Res. 24 (1979) 331-387
    • (1979) Adv. Virus Res. , vol.24 , pp. 331-387
    • Cohen, S.S.1    McCormick, F.P.2
  • 8
    • 0001679665 scopus 로고
    • Polyamine biosynthetic enzymes in Chlorella: characterization of ornithine and arginine decarboxylase
    • Cohen E., Arad S.M., Heimer Y.M., and Mizrahi Y. Polyamine biosynthetic enzymes in Chlorella: characterization of ornithine and arginine decarboxylase. Plant Cell Physiol. 24 (1983) 1003-1010
    • (1983) Plant Cell Physiol. , vol.24 , pp. 1003-1010
    • Cohen, E.1    Arad, S.M.2    Heimer, Y.M.3    Mizrahi, Y.4
  • 9
    • 0001688015 scopus 로고
    • Polyamine biosynthetic enzymes in the cell cycle of Chlorella: correlation between ornithine decarboxylase and DNA synthesis at different light intensities
    • Cohen E., Arad S.M., Heimer Y.H., and Mizrahi Y. Polyamine biosynthetic enzymes in the cell cycle of Chlorella: correlation between ornithine decarboxylase and DNA synthesis at different light intensities. Plant Physiol. 74 (1984) 385-388
    • (1984) Plant Physiol. , vol.74 , pp. 385-388
    • Cohen, E.1    Arad, S.M.2    Heimer, Y.H.3    Mizrahi, Y.4
  • 10
  • 11
    • 33846391192 scopus 로고    scopus 로고
    • Fitzgerald, L.A., Graves, M.V., Li, X., Feldblyum, T., Hartigan, J., Van Etten, J.L., in press-a. Sequence and annotation of the 314-kb MT325 and the 321-kb FR483 viruses that infect Chlorella Pbi. Virology. doi:10.1016/j.virol.2006.08.034
  • 12
    • 33846362288 scopus 로고    scopus 로고
    • Fitzgerald, L.A., Graves, M.V., Li, X., Feldblyum, T., Nierman, W.C., Van Etten, J.L., in press-b. Sequence and annotation of the 369-kb NY-2A and the 345-kb AR158 viruses that infect Chlorella NC64A. Virology.doi:10.1016/j.virol.2006.08.033
  • 13
    • 0015156237 scopus 로고
    • Compartmentalization of spermine and spermidine in the herpes simplex virion
    • Gibson W., and Roizman B. Compartmentalization of spermine and spermidine in the herpes simplex virion. Proc. Natl. Acad. Sci. U. S. A. 68 (1971) 2818-2821
    • (1971) Proc. Natl. Acad. Sci. U. S. A. , vol.68 , pp. 2818-2821
    • Gibson, W.1    Roizman, B.2
  • 14
    • 0021358189 scopus 로고
    • d,l-alpha-Difluoromethylornithine inhibits human cytomegalovirus replication
    • Gibson W., van Breemen R., Fields A., LaFemina R., and Irmiere A. d,l-alpha-Difluoromethylornithine inhibits human cytomegalovirus replication. J. Virol. 50 (1984) 145-154
    • (1984) J. Virol. , vol.50 , pp. 145-154
    • Gibson, W.1    van Breemen, R.2    Fields, A.3    LaFemina, R.4    Irmiere, A.5
  • 15
    • 84912248275 scopus 로고
    • Biphasic stimulation of polyamine biosynthesis in primary mouse kidney cells by infection with polyoma virus: uncoupling from DNA and rRNA synthesis
    • Goldstein D.A., Heby O., and Marton L.J. Biphasic stimulation of polyamine biosynthesis in primary mouse kidney cells by infection with polyoma virus: uncoupling from DNA and rRNA synthesis. Proc. Natl. Acad. Sci. U. S. A. 73 (1976) 4022-4026
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 4022-4026
    • Goldstein, D.A.1    Heby, O.2    Marton, L.J.3
  • 16
    • 21744446084 scopus 로고    scopus 로고
    • S-Adenosyl methionine decarboxylase activity is required for the outcome of herpes simplex virus type 1 infection and represents a new potential therapeutic target
    • Greco A., Calle A., Morfin F., Thouvenot D., Cayre M., Kindbeiter K., Martin L., Levillain O., and Diaz J.J. S-Adenosyl methionine decarboxylase activity is required for the outcome of herpes simplex virus type 1 infection and represents a new potential therapeutic target. FASEB J. 19 (2005) 1128-1130
    • (2005) FASEB J. , vol.19 , pp. 1128-1130
    • Greco, A.1    Calle, A.2    Morfin, F.3    Thouvenot, D.4    Cayre, M.5    Kindbeiter, K.6    Martin, L.7    Levillain, O.8    Diaz, J.J.9
  • 17
    • 0034798209 scopus 로고    scopus 로고
    • Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity
    • Hanfrey C., Sommer S., Mayer M.J., Burtin D., and Michael A.J. Arabidopsis polyamine biosynthesis: absence of ornithine decarboxylase and the mechanism of arginine decarboxylase activity. Plant J. 27 (2001) 551-560
    • (2001) Plant J. , vol.27 , pp. 551-560
    • Hanfrey, C.1    Sommer, S.2    Mayer, M.J.3    Burtin, D.4    Michael, A.J.5
  • 19
    • 0037680462 scopus 로고    scopus 로고
    • Identification and characterization of plant agmatine iminohydrolase, the last missing link in polyamine biosynthesis of plants
    • Janowitz T., Kneifel H., and Piotrowski M. Identification and characterization of plant agmatine iminohydrolase, the last missing link in polyamine biosynthesis of plants. FEBS Lett. 544 (2003) 258-261
    • (2003) FEBS Lett. , vol.544 , pp. 258-261
    • Janowitz, T.1    Kneifel, H.2    Piotrowski, M.3
  • 21
    • 1242319467 scopus 로고    scopus 로고
    • Immediate early genes expressed in chlorovirus infections
    • Kawasaki T., Tanaka M., Fujie M., Usami S., and Yamada T. Immediate early genes expressed in chlorovirus infections. Virology 318 (2004) 214-223
    • (2004) Virology , vol.318 , pp. 214-223
    • Kawasaki, T.1    Tanaka, M.2    Fujie, M.3    Usami, S.4    Yamada, T.5
  • 22
    • 0030994798 scopus 로고    scopus 로고
    • Amelioration of bacterial genomes: rates of change and exchange
    • Lawrence J.G., and Ochman H. Amelioration of bacterial genomes: rates of change and exchange. J. Mol. Evol. 44 (1997) 383-397
    • (1997) J. Mol. Evol. , vol.44 , pp. 383-397
    • Lawrence, J.G.1    Ochman, H.2
  • 24
    • 0037351889 scopus 로고    scopus 로고
    • Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway
    • Nakada Y., and Itoh Y. Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway. Microbiology 149 (2003) 707-714
    • (2003) Microbiology , vol.149 , pp. 707-714
    • Nakada, Y.1    Itoh, Y.2
  • 25
    • 0034750704 scopus 로고    scopus 로고
    • Molecular characterization and regulation of the aguBA operon, responsible for agmatine utilization in Pseudomonas aeruginosa PAO1
    • Nakada Y., Jiang Y., Nishijyo T., Itoh Y., and Lu C.D. Molecular characterization and regulation of the aguBA operon, responsible for agmatine utilization in Pseudomonas aeruginosa PAO1. J. Bacteriol. 183 (2001) 6517-6524
    • (2001) J. Bacteriol. , vol.183 , pp. 6517-6524
    • Nakada, Y.1    Jiang, Y.2    Nishijyo, T.3    Itoh, Y.4    Lu, C.D.5
  • 26
    • 0017696460 scopus 로고
    • Polyamine content of several RNA plant viruses
    • Nickerson K.W., and Lane L.C. Polyamine content of several RNA plant viruses. Virology 81 (1977) 455-459
    • (1977) Virology , vol.81 , pp. 455-459
    • Nickerson, K.W.1    Lane, L.C.2
  • 27
    • 0037449739 scopus 로고    scopus 로고
    • Plant C-N hydrolases and the identification of a plant N-carbamoylputrescine amidohydrolase involved in polyamine biosynthesis
    • Piotrowski M., Janowitz T., and Kneifel H. Plant C-N hydrolases and the identification of a plant N-carbamoylputrescine amidohydrolase involved in polyamine biosynthesis. J. Biol. Chem. 278 (2003) 1708-1712
    • (2003) J. Biol. Chem. , vol.278 , pp. 1708-1712
    • Piotrowski, M.1    Janowitz, T.2    Kneifel, H.3
  • 28
    • 0023742380 scopus 로고
    • Polyamine depletion of cells reduces the infectivity of herpes simplex virus but not the infectivity of Sindbis virus
    • Pohjanpelto P., Sekki A., Hukkanen V., and von Bonsdorff C.H. Polyamine depletion of cells reduces the infectivity of herpes simplex virus but not the infectivity of Sindbis virus. Life Sci. 42 (1988) 2011-2018
    • (1988) Life Sci. , vol.42 , pp. 2011-2018
    • Pohjanpelto, P.1    Sekki, A.2    Hukkanen, V.3    von Bonsdorff, C.H.4
  • 29
    • 0019731882 scopus 로고
    • Roles of polyamines in the replication of animal viruses
    • Raina A., Tuomi K., and Mantyjarvi R. Roles of polyamines in the replication of animal viruses. Med. Biol. 59 (1981) 428-432
    • (1981) Med. Biol. , vol.59 , pp. 428-432
    • Raina, A.1    Tuomi, K.2    Mantyjarvi, R.3
  • 30
    • 0001088966 scopus 로고
    • Studies on ultrastructure and host range of a Chlorella attacking virus
    • Reisser W., Becker B., and Klein T. Studies on ultrastructure and host range of a Chlorella attacking virus. Protoplasma 135 (1986) 162-165
    • (1986) Protoplasma , vol.135 , pp. 162-165
    • Reisser, W.1    Becker, B.2    Klein, T.3
  • 32
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist F., and Huelsenbeck J.P. MrBayes 3: Bayesian phylogenetic inference under mixed models. Bioinformatics 19 (2003) 1572-1574
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 34
    • 4143113737 scopus 로고    scopus 로고
    • Paramecium bursaria chlorella virus-1 encodes an unusual arginine decarboxylase that is a close homolog of eukaryotic ornithine decarboxylases
    • Shah R., Coleman C.S., Mir K., Baldwin J., Van Etten J.L., Grishin N.V., Pegg A.E., Stanley B.A., and Phillips M.A. Paramecium bursaria chlorella virus-1 encodes an unusual arginine decarboxylase that is a close homolog of eukaryotic ornithine decarboxylases. J. Biol. Chem. 279 (2004) 35760-35767
    • (2004) J. Biol. Chem. , vol.279 , pp. 35760-35767
    • Shah, R.1    Coleman, C.S.2    Mir, K.3    Baldwin, J.4    Van Etten, J.L.5    Grishin, N.V.6    Pegg, A.E.7    Stanley, B.A.8    Phillips, M.A.9
  • 35
    • 0005266533 scopus 로고
    • Agmatine iminohydrolase in maize
    • Smith T.A. Agmatine iminohydrolase in maize. Phytochemistry 8 (1969) 2111-2117
    • (1969) Phytochemistry , vol.8 , pp. 2111-2117
    • Smith, T.A.1
  • 36
    • 0034633831 scopus 로고    scopus 로고
    • Characterization of a β-1,3-glucanase encoded by chlorella virus PBCV-1
    • Sun L., Gurnon J.R., Adams B.J., Graves M.V., and Van Etten J.L. Characterization of a β-1,3-glucanase encoded by chlorella virus PBCV-1. Virology 276 (2000) 27-36
    • (2000) Virology , vol.276 , pp. 27-36
    • Sun, L.1    Gurnon, J.R.2    Adams, B.J.3    Graves, M.V.4    Van Etten, J.L.5
  • 37
    • 0036010676 scopus 로고    scopus 로고
    • Regulation by polyamines of ornithine decarboxylase activity and cell division in the unicellular green alga Chlamydomonas reinhardtii
    • Theiss C., Bohley P., and Voigt J. Regulation by polyamines of ornithine decarboxylase activity and cell division in the unicellular green alga Chlamydomonas reinhardtii. Plant Physiol. 128 (2002) 1470-1479
    • (2002) Plant Physiol. , vol.128 , pp. 1470-1479
    • Theiss, C.1    Bohley, P.2    Voigt, J.3
  • 38
    • 0018388843 scopus 로고
    • Synthesis and accumulation of polyamines and S-adenosylmethionine in Chinese cabbage infected by turnip yellow mosaic virus
    • Torget R., Lapi L., and Cohen S.S. Synthesis and accumulation of polyamines and S-adenosylmethionine in Chinese cabbage infected by turnip yellow mosaic virus. Biochem. Biophys. Res. Commun. 87 (1979) 1132-1139
    • (1979) Biochem. Biophys. Res. Commun. , vol.87 , pp. 1132-1139
    • Torget, R.1    Lapi, L.2    Cohen, S.S.3
  • 39
    • 0010876466 scopus 로고
    • Polyamines and the growth of pathogenic viruses
    • Goldemberg S.H., and Algranati I.D. (Eds), IRL Press, Oxford
    • Tyms A.S., Clarke J.R., Ford L., and Eloranta T. Polyamines and the growth of pathogenic viruses. In: Goldemberg S.H., and Algranati I.D. (Eds). The Biology and Chemistry of Polyamines (1990), IRL Press, Oxford 122-133
    • (1990) The Biology and Chemistry of Polyamines , pp. 122-133
    • Tyms, A.S.1    Clarke, J.R.2    Ford, L.3    Eloranta, T.4
  • 40
    • 0346599192 scopus 로고    scopus 로고
    • Unusual life style of giant chlorella viruses
    • Van Etten J.L. Unusual life style of giant chlorella viruses. Annu. Rev. Genet. 37 (2003) 153-195
    • (2003) Annu. Rev. Genet. , vol.37 , pp. 153-195
    • Van Etten, J.L.1
  • 41
    • 0020615927 scopus 로고
    • Growth cycle of a virus, PBCV-1, that infects Chlorella-like algae
    • Van Etten J.L., Burbank D.E., Xia Y., and Meints R.H. Growth cycle of a virus, PBCV-1, that infects Chlorella-like algae. Virology 126 (1983) 117-125
    • (1983) Virology , vol.126 , pp. 117-125
    • Van Etten, J.L.1    Burbank, D.E.2    Xia, Y.3    Meints, R.H.4
  • 42
    • 0021262414 scopus 로고
    • DNA synthesis in a Chlorella-like alga following infection with the virus PBCV-1
    • Van Etten J.L., Burbank D.E., Joshi J., and Meints R.H. DNA synthesis in a Chlorella-like alga following infection with the virus PBCV-1. Virology 134 (1984) 443-449
    • (1984) Virology , vol.134 , pp. 443-449
    • Van Etten, J.L.1    Burbank, D.E.2    Joshi, J.3    Meints, R.H.4
  • 43
    • 0041821504 scopus 로고    scopus 로고
    • Polyamines and plant disease
    • Walters D.R. Polyamines and plant disease. Phytochemistry 64 (2003) 97-107
    • (2003) Phytochemistry , vol.64 , pp. 97-107
    • Walters, D.R.1
  • 46
    • 0001401924 scopus 로고
    • Corn agmatine iminohydrolase. Purification and properties
    • Yanagisawa H., and Suzuki Y. Corn agmatine iminohydrolase. Purification and properties. Plant Physiol. 67 (1981) 697-700
    • (1981) Plant Physiol. , vol.67 , pp. 697-700
    • Yanagisawa, H.1    Suzuki, Y.2


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