메뉴 건너뛰기




Volumn 54, Issue 1, 2004, Pages 39-54

A small family of LLS1-related non-heme oxygenases in plants with an origin amongst oxygenic photosynthesizers

Author keywords

Acd1; Cao (chlorophyll a oxygenase); Cmo (choline monooxygenase); Dioxygenase; Lls1; Non heme oxygenase; Pao (pheophorbide a oxygenase); Ptc52; Tic55

Indexed keywords

CHLOROPHYLL; ENZYMES; PHOTOSYNTHESIS;

EID: 3442885737     PISSN: 01674412     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:PLAN.0000028766.61559.4c     Document Type: Article
Times cited : (70)

References (43)
  • 3
    • 0002557598 scopus 로고
    • Phthalate dioxygenase reductase and related flavin-iron sulfur containing electron transferases
    • Batie, C.J., Ballou, D.P. and Correll, C.C. 1991. Phthalate dioxygenase reductase and related flavin-iron sulfur containing electron transferases. Chem. Biochem. Flavoenzymes 3: 543-556.
    • (1991) Chem. Biochem. Flavoenzymes , vol.3 , pp. 543-556
    • Batie, C.J.1    Ballou, D.P.2    Correll, C.C.3
  • 4
    • 0032817545 scopus 로고    scopus 로고
    • Enzymes of chlorophyll biosynthesis
    • Beale, S.I. 1999. Enzymes of chlorophyll biosynthesis. Photosyn. Res. 60: 43-73.
    • (1999) Photosyn. Res. , vol.60 , pp. 43-73
    • Beale, S.I.1
  • 5
    • 0028855121 scopus 로고
    • Assay, purification and partial characterization of choline mononxygenase from spinach
    • Burnet, M., Lafontaine, P.J. and Hanson, A.D. 1995. Assay, purification and partial characterization of choline mononxygenase from spinach. Plant Physiol. 108: 581-588.
    • (1995) Plant Physiol. , vol.108 , pp. 581-588
    • Burnet, M.1    Lafontaine, P.J.2    Hanson, A.D.3
  • 6
    • 0031463305 scopus 로고    scopus 로고
    • The chloroplastic protein import machinery contains a Rieske-type iron-sulfur cluster and a mononuclear iron-binding protein
    • Caliebe, A., Grimm, R., Kaiser, G., Lubeck, J., Soll, J. and Heins, L. 1997. The chloroplastic protein import machinery contains a Rieske-type iron-sulfur cluster and a mononuclear iron-binding protein. EMBO J. 16: 7342-7350.
    • (1997) EMBO J. , vol.16 , pp. 7342-7350
    • Caliebe, A.1    Grimm, R.2    Kaiser, G.3    Lubeck, J.4    Soll, J.5    Heins, L.6
  • 7
    • 0029802035 scopus 로고    scopus 로고
    • Sucrose phosphate synthase expression at the cell and tissue level is coordinated with sucrose sink-to-source transitions in maize leaf
    • Cheng, W.-H., Im, K.H. and Chourey, P.S. 1996. Sucrose phosphate synthase expression at the cell and tissue level is coordinated with sucrose sink-to-source transitions in maize leaf. Plant Physiol. 111: 1021-1029.
    • (1996) Plant Physiol. , vol.111 , pp. 1021-1029
    • Cheng, W.-H.1    Im, K.H.2    Chourey, P.S.3
  • 8
    • 0030934272 scopus 로고    scopus 로고
    • The CXXC motif: A rheostat in the active site
    • Chivers, P.T., Prehoda, K.E. and Raines, R.T. 1997. The CXXC motif: a rheostat in the active site. Biochemistry 36: 4061-4066.
    • (1997) Biochemistry , vol.36 , pp. 4061-4066
    • Chivers, P.T.1    Prehoda, K.E.2    Raines, R.T.3
  • 9
    • 0033621182 scopus 로고    scopus 로고
    • The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyllb synthesis in Arabidopsis thaliana
    • Espineda, C.E., Linford, A.S., Devine, D. and Brusslan, J.A. 1999. The AtCAO gene, encoding chlorophyll a oxygenase, is required for chlorophyllb synthesis in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 96: 10507-10511.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10507-10511
    • Espineda, C.E.1    Linford, A.S.2    Devine, D.3    Brusslan, J.A.4
  • 10
    • 0030891317 scopus 로고    scopus 로고
    • A novel suppressor of cell death in plants encoded by the Lls1 gene of maize
    • Gray, J., Close, P.S., Briggs, S.P. and Johal, G.S. 1997. A novel suppressor of cell death in plants encoded by the Lls1 gene of maize. Cell 89: 25-31.
    • (1997) Cell , vol.89 , pp. 25-31
    • Gray, J.1    Close, P.S.2    Briggs, S.P.3    Johal, G.S.4
  • 11
    • 0036914512 scopus 로고    scopus 로고
    • Light-dependent death of maize lls1 cells is mediated by mature chloroplasts
    • Gray, J., Janick-Buckner, D., Buckner, B., Close, P.S. and Johal, G.S. 2002. Light-dependent death of maize lls1 cells is mediated by mature chloroplasts. Plant Physiol. 130: 1-14.
    • (2002) Plant Physiol. , vol.130 , pp. 1-14
    • Gray, J.1    Janick-Buckner, D.2    Buckner, B.3    Close, P.S.4    Johal, G.S.5
  • 13
    • 0026805891 scopus 로고
    • Functional and evolutionary relationships among diverse oxygenases
    • Harayama, S., Kok, M. and Neidle, E.L. 1992. Functional and evolutionary relationships among diverse oxygenases. Annu. Rev. Microbiol. 46: 565-601.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 565-601
    • Harayama, S.1    Kok, M.2    Neidle, E.L.3
  • 15
    • 0036829814 scopus 로고    scopus 로고
    • Functional characterization of choline monooxygenase, an enzyme for betaine synthesis in plants
    • Hibino, T., Waditee, R., Araki, E., Ishiwaka, H., Kenji, A., Tanaka, Y. and Takebe, T., 2002. Functional characterization of choline monooxygenase, an enzyme for betaine synthesis in plants. J. Biol. Chem. 277: 41352-41360.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41352-41360
    • Hibino, T.1    Waditee, R.2    Araki, E.3    Ishiwaka, H.4    Kenji, A.5    Tanaka, Y.6    Takebe, T.7
  • 16
    • 0033569362 scopus 로고    scopus 로고
    • Chlorophyll breakdown in higher plants and algae
    • Hortensteiner, S., 1999. Chlorophyll breakdown in higher plants and algae. Cell. Mol. Life Sci. 56: 330-347.
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 330-347
    • Hortensteiner, S.1
  • 17
    • 0343618696 scopus 로고    scopus 로고
    • Chlorophyll breakdown in Chlorella protothecoides: Characterization of degreening and cloning of degreening-related genes
    • Hortensteiner, S., Chinner, J., Matile, P., Thomas, H. and Donnison, I.S. 2000. Chlorophyll breakdown in Chlorella protothecoides: characterization of degreening and cloning of degreening-related genes. Plant Mol. Biol. 42: 439-450.
    • (2000) Plant Mol. Biol. , vol.42 , pp. 439-450
    • Hortensteiner, S.1    Chinner, J.2    Matile, P.3    Thomas, H.4    Donnison, I.S.5
  • 18
    • 0033494263 scopus 로고    scopus 로고
    • Accumulation of glycinebetaine and its synthesis from radioactive precursors under salt-stress in the cyanobacterium Aphanothece halophytica
    • Incharoensakdi, A. and Wutipraditkul, N. 1999. Accumulation of glycinebetaine and its synthesis from radioactive precursors under salt-stress in the cyanobacterium Aphanothece halophytica. J. Appl. Phycol. 11: 515-523.
    • (1999) J. Appl. Phycol. , vol.11 , pp. 515-523
    • Incharoensakdi, A.1    Wutipraditkul, N.2
  • 19
    • 0029953163 scopus 로고    scopus 로고
    • Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: Potential mononuclear non-heme iron coordination sites
    • Jiang, H., Parales, R.E., Lynch, N.A. and Gibson, D.T., 1996. Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: potential mononuclear non-heme iron coordination sites. J. Bact. 178: 3133-3139.
    • (1996) J. Bact. , vol.178 , pp. 3133-3139
    • Jiang, H.1    Parales, R.E.2    Lynch, N.A.3    Gibson, D.T.4
  • 20
    • 0347264753 scopus 로고    scopus 로고
    • Crystal structure of naphthalene dioxygenase: Side-on binding of dioxygen to iron
    • Karlsson, A., Parales, J.V., Parales, R.E., Gibbon, D.T., Eklund, H. and Ramaswamy, S. 2003. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Science 299: 1039-1042.
    • (2003) Science , vol.299 , pp. 1039-1042
    • Karlsson, A.1    Parales, J.V.2    Parales, R.E.3    Gibbon, D.T.4    Eklund, H.5    Ramaswamy, S.6
  • 21
    • 0032524127 scopus 로고    scopus 로고
    • Structure of an aromatic-ring-hydroxylating dioxygenase - Naphthalene 1,2 dioxygenase
    • Kauppi, B., Lee, K., Carredano, E., Parales, R., Gibson, D.T., Eklund, H. and Ramaswamy, S. 1998. Structure of an aromatic-ring-hydroxylating dioxygenase - naphthalene 1,2 dioxygenase. Structure 6: 571-586.
    • (1998) Structure , vol.6 , pp. 571-586
    • Kauppi, B.1    Lee, K.2    Carredano, E.3    Parales, R.4    Gibson, D.T.5    Eklund, H.6    Ramaswamy, S.7
  • 22
    • 0033106153 scopus 로고    scopus 로고
    • Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway
    • Kobayashi, T. and Ito, K., 1999. Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway. EMBO J. 18: 1192-1198.
    • (1999) EMBO J. , vol.18 , pp. 1192-1198
    • Kobayashi, T.1    Ito, K.2
  • 23
    • 0037112789 scopus 로고    scopus 로고
    • Portein import into chloroplasts involves redox-regulated proteins
    • Küchler, M., Decker, S., Hörmann, F., Soll, J. and Heins, L. 2002. Portein import into chloroplasts involves redox-regulated proteins. EMBO J. 21: 6136-6145.
    • (2002) EMBO J. , vol.21 , pp. 6136-6145
    • Küchler, M.1    Decker, S.2    Hörmann, F.3    Soll, J.4    Heins, L.5
  • 24
    • 0035726624 scopus 로고    scopus 로고
    • Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation
    • Kuge, S., Arita, M., Murayama, A., Maeta, K., Izawa, S., Inoue, Y. and Nomoto, A. 2001. Regulation of the yeast Yap1p nuclear export signal is mediated by redox signal-induced reversible disulfide bond formation. Mol. Cell. Biol. 21: 6139-6150.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6139-6150
    • Kuge, S.1    Arita, M.2    Murayama, A.3    Maeta, K.4    Izawa, S.5    Inoue, Y.6    Nomoto, A.7
  • 25
    • 0032039677 scopus 로고    scopus 로고
    • Oxygen activating nonheme iron enzymes
    • Lange, S.J. and Que, L. Jr. 1998. Oxygen activating nonheme iron enzymes. Curr. Opin. Chem. Biol. 2: 159-172.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 159-172
    • Lange, S.J.1    Que Jr., L.2
  • 26
    • 0026743341 scopus 로고
    • The electron-transport proteins of hydroxylating bacterial dioxygenases
    • Mason, J.R. and Cammack, R. 1992. The electron-transport proteins of hydroxylating bacterial dioxygenases. Annu. Rev. Microbiol. 46: 277-305.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 277-305
    • Mason, J.R.1    Cammack, R.2
  • 27
    • 0017689479 scopus 로고
    • Effect of carbon dioxide on pigment and membrane content in Synechococcus lividus
    • Miller, L.S. and Holt, S.C. 1977. Effect of carbon dioxide on pigment and membrane content in Synechococcus lividus. Arch. Microbiol. 115: 185-198.
    • (1977) Arch. Microbiol. , vol.115 , pp. 185-198
    • Miller, L.S.1    Holt, S.C.2
  • 28
    • 0033981219 scopus 로고    scopus 로고
    • Substrate range and genetic analysis of Acinetobacter vanillate demethylase
    • Moraswki, B., Segura, A. and Ornston, L.N. 2000. Substrate range and genetic analysis of Acinetobacter vanillate demethylase. J. Bact. 182: 1383-1389.
    • (2000) J. Bact. , vol.182 , pp. 1383-1389
    • Moraswki, B.1    Segura, A.2    Ornston, L.N.3
  • 29
    • 0034604170 scopus 로고    scopus 로고
    • The origin of red algae and the evolution of chloroplasts
    • Moreira, D., Guyader, H.L. and Phillipe, H. 2000. The origin of red algae and the evolution of chloroplasts. Nature 405: 69-72.
    • (2000) Nature , vol.405 , pp. 69-72
    • Moreira, D.1    Guyader, H.L.2    Phillipe, H.3
  • 30
    • 0035257614 scopus 로고    scopus 로고
    • New classification system for oxygenase components involved in ring-hydroxylating oxygenations
    • Nam, J.-W., Nojiri, H., Yoshida, T., Habe, H., Yamane, H. and Omori, T. 2001. New classification system for oxygenase components involved in ring-hydroxylating oxygenations. Biosci. Biotechnol. Biochem. 65: 254-263.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 254-263
    • Nam, J.-W.1    Nojiri, H.2    Yoshida, T.3    Habe, H.4    Yamane, H.5    Omori, T.6
  • 31
    • 0026017943 scopus 로고
    • Nueleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases
    • Neidle, E.L., Hartnett, C., Ornston, L.N., Bairoch, A., Rekik, M. and Harayama, S. 1991. Nueleotide sequences of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among multicomponent oxygenases. J. Bact. 173: 5385-5395.
    • (1991) J. Bact. , vol.173 , pp. 5385-5395
    • Neidle, E.L.1    Hartnett, C.2    Ornston, L.N.3    Bairoch, A.4    Rekik, M.5    Harayama, S.6
  • 32
    • 0033854668 scopus 로고    scopus 로고
    • The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism
    • Prescott, A.G. and Lloyd, M.D. 2000. The iron(II) and 2-oxoacid-dependent dioxygenases and their role in metabolism. Nat. Prod. Rep. 17: 367-383.
    • (2000) Nat. Prod. Rep. , vol.17 , pp. 367-383
    • Prescott, A.G.1    Lloyd, M.D.2
  • 33
    • 0030970522 scopus 로고    scopus 로고
    • Chorine monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning
    • Rathinasabapathi, B., Burnet, M., Russell, B.L., Gage, D.A., Liao, P.-C., Nye, G.J., Scott, P., Golbeck, J.H. and Hanson, A.D. 1997. Chorine monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: prosthetic group characterization and cDNA cloning. Proc. Natl. Acad. Sci. USA 94: 3454-3458.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3454-3458
    • Rathinasabapathi, B.1    Burnet, M.2    Russell, B.L.3    Gage, D.A.4    Liao, P.-C.5    Nye, G.J.6    Scott, P.7    Golbeck, J.H.8    Hanson, A.D.9
  • 34
    • 0035036517 scopus 로고    scopus 로고
    • Nitrogen or sulfur starvation differentially affects phycobilisome degradation and expression of the nb1A gene in Synechocystis strain PCC 6803
    • Richaud, C., Zabulon, G., Joder, A. and Thomas, J.-C., 2001. Nitrogen or sulfur starvation differentially affects phycobilisome degradation and expression of the nb1A gene in Synechocystis strain PCC 6803. J. Bact. 183: 2989-2994.
    • (2001) J. Bact. , vol.183 , pp. 2989-2994
    • Richaud, C.1    Zabulon, G.2    Joder, A.3    Thomas, J.-C.4
  • 35
    • 0029151963 scopus 로고
    • Metabolic pathway for glycerol synthesis under osmotic stress in the freshwater green alga Chlamydomonas reinhardtii
    • Rosa, L. and Galvan, F. 1995. Metabolic pathway for glycerol synthesis under osmotic stress in the freshwater green alga Chlamydomonas reinhardtii. Plant Physiol. Biochem. 33: 213-218.
    • (1995) Plant Physiol. Biochem. , vol.33 , pp. 213-218
    • Rosa, L.1    Galvan, F.2
  • 36
    • 0032415127 scopus 로고    scopus 로고
    • Analysis of the chlorophyll biosynthetic system in a chlorophyll b-less barley mutant
    • Rudoi, A.B. and Shcherbakov, R.A., 1998. Analysis of the chlorophyll biosynthetic system in a chlorophyll b-less barley mutant. Photosyn. Res. 58: 71-80.
    • (1998) Photosyn. Res. , vol.58 , pp. 71-80
    • Rudoi, A.B.1    Shcherbakov, R.A.2
  • 38
    • 0032514698 scopus 로고    scopus 로고
    • Chlorophyll a oxygenase is involved in chlorophyll b formation from chlorophyll a
    • Tanaka, A., Ito, H., Tanaka, R., Tanaka, N., Yoshida, K. and Okada, K. 1998. Chlorophyll a oxygenase is involved in chlorophyll b formation from chlorophyll a. Proc. Natl. Acad. Sci. USA 95: 12719-12723.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12719-12723
    • Tanaka, A.1    Ito, H.2    Tanaka, R.3    Tanaka, N.4    Yoshida, K.5    Okada, K.6
  • 39
    • 0034943675 scopus 로고    scopus 로고
    • Overexpression of chlorophyllide a oxygenase (CAO) enlarges the antenna size of photosystem II in Arabidopsis thaliana
    • Tanaka, R., Koshino, Y., Sawa, S., Ishiguro, S., Okada, K. and Tanaka, A. 2001. Overexpression of chlorophyllide a oxygenase (CAO) enlarges the antenna size of photosystem II in Arabidopsis thaliana. Plant J. 26: 365-373.
    • (2001) Plant J. , vol.26 , pp. 365-373
    • Tanaka, R.1    Koshino, Y.2    Sawa, S.3    Ishiguro, S.4    Okada, K.5    Tanaka, A.6
  • 40
    • 0036498845 scopus 로고    scopus 로고
    • Cyanobacterial photosynthesis in the oceans: The origins and significance of divergent light-harvesting strategies
    • Ting, C.S., Rocap, G., King, J. and Chisholm, S.W. 2002. Cyanobacterial photosynthesis in the oceans: the origins and significance of divergent light-harvesting strategies. Trends Microbiol. 10: 134-142.
    • (2002) Trends Microbiol. , vol.10 , pp. 134-142
    • Ting, C.S.1    Rocap, G.2    King, J.3    Chisholm, S.W.4
  • 41
    • 0033536171 scopus 로고    scopus 로고
    • Chlorophyll b and phycobilins in the common ancestor of cyanobacteria and chloroplasts
    • Tomitani, A., Okada, K., Miyashita, H., Matthijs, H.C. and Ohno, T. 1999. Chlorophyll b and phycobilins in the common ancestor of cyanobacteria and chloroplasts. Nature 400: 159-162.
    • (1999) Nature , vol.400 , pp. 159-162
    • Tomitani, A.1    Okada, K.2    Miyashita, H.3    Matthijs, H.C.4    Ohno, T.5
  • 42
    • 3442887462 scopus 로고    scopus 로고
    • The wound-inducible Lls1 gene from maize is an ortholog of the Arabidopsis Acd1 gene, and the LLS1 protein is present in non-photosynthetic tissues
    • Yang, M., Wardzala, E., Johal, G.S. and Gray, J. 2004. The wound-inducible Lls1 gene from maize is an ortholog of the Arabidopsis Acd1 gene, and the LLS1 protein is present in non-photosynthetic tissues. Plant Mol Biol. 54: 175-191.
    • (2004) Plant Mol. Biol. , vol.54 , pp. 175-191
    • Yang, M.1    Wardzala, E.2    Johal, G.S.3    Gray, J.4
  • 43
    • 0036744350 scopus 로고    scopus 로고
    • Disulfide proteome in the analysis of protein function and structure
    • Yano, H., Kuroda, S. and Buchanan, B.B. 2002. Disulfide proteome in the analysis of protein function and structure. Proteomics 2: 1090-1096.
    • (2002) Proteomics , vol.2 , pp. 1090-1096
    • Yano, H.1    Kuroda, S.2    Buchanan, B.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.