메뉴 건너뛰기




Volumn 289, Issue 3, 2014, Pages 1841-1851

A novel "oxygen-induced" greening process in a cyanobacterial mutant lacking the transcriptional activator ChlR involved in low-oxygen adaptation of tetrapyrrole biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ALTERNATIVE SYSTEMS; CYANOBACTERIUM SYNECHOCYSTIS; FLUORESCENCE SPECTRA; LOW TEMPERATURES; OXYGEN-DEPENDENT REACTIONS; PHOTOAUTOTROPHIC GROWTH; TRANSCRIPTIONAL ACTIVATORS; WESTERN BLOTTING;

EID: 84892668033     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.495358     Document Type: Article
Times cited : (13)

References (38)
  • 1
    • 79958107010 scopus 로고    scopus 로고
    • Chlorophyll cycle regulates the construction and destruction of the light-harvesting complexes
    • Tanaka, R., and Tanaka, A. (2011) Chlorophyll cycle regulates the construction and destruction of the light-harvesting complexes. Biochim. Biophys. Acta 1807, 968-976
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 968-976
    • Tanaka, R.1    Tanaka, A.2
  • 2
    • 53749102865 scopus 로고    scopus 로고
    • Regulation and evolution of chlorophyll metabolism
    • Masuda, T., and Fujita, Y. (2008) Regulation and evolution of chlorophyll metabolism. Photochem. Photobiol. Sci. 7, 1131-1149
    • (2008) Photochem. Photobiol. Sci. , vol.7 , pp. 1131-1149
    • Masuda, T.1    Fujita, Y.2
  • 3
    • 84857983500 scopus 로고    scopus 로고
    • Post-translational control of tetrapyrrole biosynthesis in plants, algae, and cyanobacteria
    • Czarnecki, O., and Grimm, B. (2012) Post-translational control of tetrapyrrole biosynthesis in plants, algae, and cyanobacteria. J. Exp. Bot. 63, 1675-1687
    • (2012) J. Exp. Bot. , vol.63 , pp. 1675-1687
    • Czarnecki, O.1    Grimm, B.2
  • 4
    • 34250807129 scopus 로고    scopus 로고
    • Tetrapyrrole biosynthesis in higher plants
    • DOI 10.1146/annurev.arplant.57.032905.105448
    • Tanaka, R., and Tanaka, A. (2007) Tetrapyrrole biosynthesis in higher plants. Annu. Rev. Plant Biol. 58, 321-346 (Pubitemid 46986328)
    • (2007) Annual Review of Plant Biology , vol.58 , pp. 321-346
    • Tanaka, R.1    Tanaka, A.2
  • 5
    • 0030175228 scopus 로고    scopus 로고
    • Protochlorophyllide reduction: A key step in the greening of plants
    • Fujita, Y. (1996) Protochlorophyllide reduction: a key step in the greening of plants. Plant Cell Physiol. 37, 411-421 (Pubitemid 26351701)
    • (1996) Plant and Cell Physiology , vol.37 , Issue.4 , pp. 411-421
    • Fujita, Y.1
  • 7
    • 3242883632 scopus 로고    scopus 로고
    • Novel insights into the enzymology, regulation and physiological functions of light-dependent protochlorophyllide oxidoreductase in angiosperms
    • DOI 10.1023/B:PRES.0000028392.80354.7c
    • Masuda, T., and Takamiya, K. (2004) Novel insights into the enzymology, regulation and physiological funcitons of light-dependent protochlorophyllide oxidoreductase in angiosperms. Photosynth. Res. 81, 1-29 (Pubitemid 38995172)
    • (2004) Photosynthesis Research , vol.81 , Issue.1 , pp. 1-29
    • Masuda, T.1    Takamiya, K.-I.2
  • 9
    • 79957828506 scopus 로고    scopus 로고
    • Biogenesis of thylakoid networks in angiosperms: Knowns and unknowns
    • Adam, Z., Charuvi, D., Tsabari, O., Knopf, R. R., and Reich, Z. (2011) Biogenesis of thylakoid networks in angiosperms: knowns and unknowns. Plant Mol. Biol. 76, 221-234
    • (2011) Plant Mol. Biol. , vol.76 , pp. 221-234
    • Adam, Z.1    Charuvi, D.2    Tsabari, O.3    Knopf, R.R.4    Reich, Z.5
  • 10
    • 0038025174 scopus 로고    scopus 로고
    • Assembly of the D1 precursor in monomeric photosystem II reaction center precomplexes precedes chlorophyll a-triggered accumulation of reaction center II in barley etioplasts
    • DOI 10.1105/tpc.11.12.2365
    • Müller, B., and Eichacker, L. A. (1999) Assembly of the D1 precursor in monomeric photosystem II reaction center precomplexes precedes chlorophyll a-triggered accumulation of reaction center II in barley etioplasts. Plant Cell 11, 2365-2377 (Pubitemid 30031381)
    • (1999) Plant Cell , vol.11 , Issue.12 , pp. 2365-2377
    • Muller, B.1    Eichacker, L.A.2
  • 11
    • 0034022990 scopus 로고    scopus 로고
    • Yellow-in-The-dark mutants of Chlamydomonas lack the CHLL subunit of light-independent protochlorophyllide reductase
    • DOI 10.1105/tpc.12.4.559
    • Cahoon, A. B., and Timko, M. P. (2000) yellow-in-the-dark mutants of Chlamydomonas lack the CHLL subunit of light-independent protochlorophyllide reductase. Plant Cell 12, 559-568 (Pubitemid 30254872)
    • (2000) Plant Cell , vol.12 , Issue.4 , pp. 559-568
    • Cahoon, A.B.1    Timko, M.P.2
  • 12
    • 0014753152 scopus 로고
    • Biogenesis of chloroplast membranes. IV. Lipid and pigment changes during synthesis of chloroplast membranes in a mutant of Chlamydomonas reinhardi y-1
    • Goldberg, I., and Ohad, I. (1970) Biogenesis of chloroplast membranes. IV. Lipid and pigment changes during synthesis of chloroplast membranes in a mutant of Chlamydomonas reinhardi y-1. J. Cell Biol. 44, 563-571
    • (1970) J. Cell Biol. , vol.44 , pp. 563-571
    • Goldberg, I.1    Ohad, I.2
  • 13
    • 0016375921 scopus 로고
    • Biogenesis and modulation of membrane properties in greening Chlamydomonas reinhardi, y-1 cells
    • Ohad, I. (1974) Biogenesis and modulation of membrane properties in greening Chlamydomonas reinhardi, y-1 cells. Methods Enzymol. 32, 865-871
    • (1974) Methods Enzymol. , vol.32 , pp. 865-871
    • Ohad, I.1
  • 14
    • 0016989304 scopus 로고
    • Kinetics and regulation of synthesis of the major polypeptides of thylakoid membranes in Chlamydomonas reinhardtii y-1 at elevated temperatures
    • Hoober, J. K., and Stegeman, W. J. (1976) Kinetics and regulation of synthesis of the major polypeptides of thylakoid membranes in Chlamydomonas reinhardtii y-1 at elevated temperatures. J. Cell Biol. 70, 326-337
    • (1976) J. Cell Biol. , vol.70 , pp. 326-337
    • Hoober, J.K.1    Stegeman, W.J.2
  • 15
    • 57849098049 scopus 로고    scopus 로고
    • Chloroplast-encoded PsbT is required for efficient biogenesis of photosystem II complex in the green alga Chlamydomonas reinhardtii
    • DOI 10.1007/s11120-008-9344-8
    • Ohnishi, N., and Takahashi, Y. (2008) Chloroplast-encoded PsbT is required for efficient biogenesis of photosystem II complex in the green alga Chlamydomonas reinhardtii. Photosynth. Res. 98, 315-322 (Pubitemid 50242694)
    • (2008) Photosynthesis Research , vol.98 , Issue.1-3 , pp. 315-322
    • Ohnishi, N.1    Takahashi, Y.2
  • 16
    • 0001916527 scopus 로고
    • The nifH-like (frxC) gene is involved in the biosynthesis of chlorophyll in the filamentous cyanobacterium Plectonema boryanum
    • Fujita, Y., Takahashi, Y., Chuganji, M., and Matsubara, H. (1992) The nifH-like (frxC) gene is involved in the biosynthesis of chlorophyll in the filamentous cyanobacterium Plectonema boryanum. Plant Cell Physiol. 33, 81-92
    • (1992) Plant Cell Physiol. , vol.33 , pp. 81-92
    • Fujita, Y.1    Takahashi, Y.2    Chuganji, M.3    Matsubara, H.4
  • 17
    • 0029557009 scopus 로고
    • Light-dependent chlorophyll a biosynthesis upon chlL deletion in wild-type and Photosystem I-less strains of the cyanobacterium Synechocystis sp. PCC 6803
    • Wu, Q., and Vermaas, W. F. (1995) Light-dependent chlorophyll a biosynthesis upon chlL deletion in wild-type and photosystem I-less strains of the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol. Biol. 29, 933-945 (Pubitemid 3020805)
    • (1995) Plant Molecular Biology , vol.29 , Issue.5 , pp. 933-945
    • Wu Qingyu1    Vermaas, W.F.2
  • 18
    • 0037276001 scopus 로고    scopus 로고
    • Arrest of chlorophyll synthesis and differential decrease of photosystems I and II in a cyanobacterial mutant lacking light-independent protochlorophyllide reductase
    • DOI 10.1023/A:1021195226978
    • Kada, S., Koike, H., Satoh, K., Hase, T., and Fujita, Y. (2003) Arrest of chlorophyll synthesis and differential decrease of Photosystems I and II in a cyanobacterial mutant lacking light-independent protochlorophyllide reductase. Plant Mol. Biol. 51, 225-235 (Pubitemid 36189187)
    • (2003) Plant Molecular Biology , vol.51 , Issue.2 , pp. 225-235
    • Kada, S.1    Koike, H.2    Satoh, K.3    Hase, T.4    Fujita, Y.5
  • 19
    • 84873086945 scopus 로고    scopus 로고
    • Inhibition of chlorophyll biosynthesis at the protochlorophyllide reduction step results in the parallel depletion of Photosystem i and Photosystem II in the cyanobacterium Synechocystis PCC 6803
    • Kopečná, J., Sobotka, R., and Komenda, J. (2013) Inhibition of chlorophyll biosynthesis at the protochlorophyllide reduction step results in the parallel depletion of Photosystem I and Photosystem II in the cyanobacterium Synechocystis PCC 6803. Planta 237, 497-508
    • (2013) Planta , vol.237 , pp. 497-508
    • Kopečná, J.1    Sobotka, R.2    Komenda, J.3
  • 20
    • 77952916829 scopus 로고    scopus 로고
    • Functional differentiation of two analogous coproporphyrinogen III oxidases for heme and chlorophyll biosynthesis pathways in the cyanobacterium Synechocystis sp. PCC 6803
    • Goto, T., Aoki, R., Minamizaki, K., and Fujita, Y. (2010) Functional differentiation of two analogous coproporphyrinogen III oxidases for heme and chlorophyll biosynthesis pathways in the cyanobacterium Synechocystis sp. PCC 6803. Plant Cell Physiol. 51, 650-663
    • (2010) Plant Cell Physiol. , vol.51 , pp. 650-663
    • Goto, T.1    Aoki, R.2    Minamizaki, K.3    Fujita, Y.4
  • 21
    • 0031666414 scopus 로고    scopus 로고
    • Analogous enzymes: Independent inventions in enzyme evolution
    • Galperin, M. Y., Walker, D. R., and Koonin, E. V. (1998) Analogous enzymes: independent inventions in enzyme evolution. Genome Res. 8, 779-790 (Pubitemid 28458280)
    • (1998) Genome Research , vol.8 , Issue.8 , pp. 779-790
    • Galperin, M.Y.1    Walker, D.R.2    Koonin, E.V.3
  • 22
    • 41449093999 scopus 로고    scopus 로고
    • Identification of two homologous genes, chlAI and chlAII, that are differentially involved in isocyclic ring formation of chlorophyll a in the cyanobacterium Synechocystis sp. PCC 6803
    • Minamizaki, K., Mizoguchi, T., Goto, T., Tamiaki, H., and Fujita, Y. (2008) Identification of two homologous genes, chlAI and chlAII, that are differentially involved in isocyclic ring formation of chlorophyll a in the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem. 283, 2684-2692
    • (2008) J. Biol. Chem. , vol.283 , pp. 2684-2692
    • Minamizaki, K.1    Mizoguchi, T.2    Goto, T.3    Tamiaki, H.4    Fujita, Y.5
  • 23
    • 80054705660 scopus 로고    scopus 로고
    • A heme oxygenase isoform is essential for aerobic growth in the cyanobacterium Synechocystis sp. PCC 6803: Modes of differential operation of two isoforms/enzymes to adapt to low oxygen environments in cyanobacteria
    • Aoki, R., Goto, T., and Fujita, Y. (2011) A heme oxygenase isoform is essential for aerobic growth in the cyanobacterium Synechocystis sp. PCC 6803: Modes of differential operation of two isoforms/enzymes to adapt to low oxygen environments in cyanobacteria. Plant Cell Physiol. 52, 1744-1756
    • (2011) Plant Cell Physiol. , vol.52 , pp. 1744-1756
    • Aoki, R.1    Goto, T.2    Fujita, Y.3
  • 24
    • 84859773974 scopus 로고    scopus 로고
    • MarR-type transcriptional regulator ChlR activates expression of tetrapyrrole biosynthesis genes in response to low-oxygen conditions in cyanobacteria
    • Aoki, R., Takeda, T., Omata, T., Ihara, K., and Fujita, Y. (2012) MarR-type transcriptional regulator ChlR activates expression of tetrapyrrole biosynthesis genes in response to low-oxygen conditions in cyanobacteria. J. Biol. Chem. 287, 13500-13507
    • (2012) J. Biol. Chem. , vol.287 , pp. 13500-13507
    • Aoki, R.1    Takeda, T.2    Omata, T.3    Ihara, K.4    Fujita, Y.5
  • 25
    • 57449108112 scopus 로고    scopus 로고
    • Low-oxygen induction of normally cryptic psbA genes in cyanobacteria
    • Summerfield, T. C., Toepel, J., and Sherman, L. A. (2008) Low-oxygen induction of normally cryptic psbA genes in cyanobacteria. Biochemistry 47, 12939-12941
    • (2008) Biochemistry , vol.47 , pp. 12939-12941
    • Summerfield, T.C.1    Toepel, J.2    Sherman, L.A.3
  • 26
    • 33744959925 scopus 로고    scopus 로고
    • A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: Reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus
    • DOI 10.1074/jbc.M601750200
    • Nomata, J., Mizoguchi, T., Tamiaki, H., and Fujita, Y. (2006) A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus. J. Biol. Chem. 281, 15021-15028 (Pubitemid 43855206)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.21 , pp. 15021-15028
    • Nomata, J.1    Mizoguchi, T.2    Tamiaki, H.3    Fujita, Y.4
  • 27
    • 33751079088 scopus 로고    scopus 로고
    • Differential operation of dual protochlorophyllide reductases for chlorophyll biosynthesis in response to environmental oxygen levels in the cyanobacterium Leptolyngbya boryana
    • DOI 10.1104/pp.106.086090
    • Yamazaki, S., Nomata, J., and Fujita, Y. (2006) Differential operation of dual protochlorophyllide reductases for chlorophyll biosynthesis in response to environmental oxygen levels in the cyanobacterium Leptolyngbya boryana. Plant Physiol. 142, 911-922 (Pubitemid 44764619)
    • (2006) Plant Physiology , vol.142 , Issue.3 , pp. 911-922
    • Yamazaki, S.1    Nomata, J.2    Fujita, Y.3
  • 28
    • 0034737351 scopus 로고    scopus 로고
    • 8 column and pyridine-containing mobile phases
    • Zapata, M., Rodoriguez, R., and Garrido, J. L. (2000) Separation of chlorophylls and carotenoids from marine phytoplankton: a new HPLC method using a reversed phase C8 column and pyridine-containing mobile phases. Marine-Ecology-Progress Series 195, 29-45 (Pubitemid 30221208)
    • (2000) Marine Ecology Progress Series , vol.195 , pp. 29-45
    • Zapata, M.1    Rodriguez, F.2    Garrido, J.L.3
  • 29
    • 0001579901 scopus 로고
    • Regulation of the stoichiometry of thylakoid components in the photosynthetic system of cyanophytes: Model experiments showing that control of the synthesis or supply of Chl a can change the stoichiometric relationship between the two photosystems
    • Fujita, Y., Murakami, A., and Ohki, K. (1990) Regulation of the stoichiometry of thylakoid components in the photosynthetic system of cyanophytes: Model experiments showing that control of the synthesis or supply of Chl a can change the stoichiometric relationship between the two photosystems. Plant Cell Physiol. 31, 145-153
    • (1990) Plant Cell Physiol. , vol.31 , pp. 145-153
    • Fujita, Y.1    Murakami, A.2    Ohki, K.3
  • 30
    • 0001231299 scopus 로고
    • Stoichiometry of system i and system II reaction centers and of plastoquinone in different photosynthetic membranes
    • Melis, A., and Brown, J. S. (1980) Stoichiometry of system I and system II reaction centers and of plastoquinone in different photosynthetic membranes. Proc. Natl. Acad. Sci. U.S.A. 77, 4712-4716
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 4712-4716
    • Melis, A.1    Brown, J.S.2
  • 31
    • 84861693795 scopus 로고    scopus 로고
    • Assembling and maintaining the photosystem II complex in chloroplasts and cyanobacteria
    • Komenda, J., Sobotka, R., and Nixon, P. J. (2012) Assembling and maintaining the photosystem II complex in chloroplasts and cyanobacteria. Curr. Opin. Plant Biol. 15, 245-251
    • (2012) Curr. Opin. Plant Biol. , vol.15 , pp. 245-251
    • Komenda, J.1    Sobotka, R.2    Nixon, P.J.3
  • 34
    • 0028090388 scopus 로고
    • Purification and partial characterisation of barley glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to chlorophyll biosynthesis
    • DOI 10.1111/j.1432-1033.1994.00529.x
    • Pontoppidan, B., and Kannangara, C. G. (1994) Purification and partial characterisation of barley glutamyl-tRNAGlu reductase, the enzyme that directs glutamate to chlorophyll biosynthesis. Eur. J. Biochem. 225, 529-537 (Pubitemid 24325569)
    • (1994) European Journal of Biochemistry , vol.225 , Issue.2 , pp. 529-537
    • Pontoppidan, B.1    Kannangara, C.G.2
  • 35
    • 0029787019 scopus 로고    scopus 로고
    • Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase
    • Vothknecht, U. C., Kannangara, C. G., and von Wettstein, D. (1996) Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase. Proc. Natl. Acad. Sci. U.S.A. 93, 9287-9291
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 9287-9291
    • Vothknecht, U.C.1    Kannangara, C.G.2    Von Wettstein, D.3
  • 37
    • 47849127156 scopus 로고    scopus 로고
    • NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are needed for the protection of Mg-protoporphyrin monomethyl ester cyclase
    • Stenbaek, A., Hansson, A., Wulff, R. P., Hansson, M., Dietz, K. J., and Jensen, P. E. (2008) NADPH-dependent thioredoxin reductase and 2-Cys peroxiredoxins are needed for the protection of Mg-protoporphyrin monomethyl ester cyclase. FEBS Lett. 582, 2773-2778
    • (2008) FEBS Lett. , vol.582 , pp. 2773-2778
    • Stenbaek, A.1    Hansson, A.2    Wulff, R.P.3    Hansson, M.4    Dietz, K.J.5    Jensen, P.E.6
  • 38
    • 4444342898 scopus 로고    scopus 로고
    • Gene expression profiling of the tetrapyrrole metabolic pathway in arabidopsis with a mini-array system
    • DOI 10.1104/pp.104.042408
    • Matsumoto, F., Obayashi, T., Sasaki-Sekimoto, Y., Ohta, H., Takamiya, K., and Masuda, T. (2004) Gene expression profiling of the tetrapyrrole metabolic pathway in Arabidopsis with a mini-array system. Plant Physiol. 135, 2379-2391 (Pubitemid 39182813)
    • (2004) Plant Physiology , vol.135 , Issue.4 , pp. 2379-2391
    • Matsumoto, F.1    Obayashi, T.2    Sasaki-Sekimoto, Y.3    Ohta, H.4    Takamiya, K.-I.5    Masuda, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.