메뉴 건너뛰기




Volumn 7, Issue 1, 2014, Pages 87-100

Redox regulation of glycogen biosynthesis in the cyanobacterium synechocystis sp. PCC 6803: Analysis of the AGP and glycogen synthases

Author keywords

Cyanobacteria; Glycogen; Redox regulation; Synechocystis; Thioredoxin

Indexed keywords

CYSTEINE; GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE; GLYCOGEN; GLYCOGEN SYNTHASE; THIOREDOXIN;

EID: 84891767260     PISSN: 16742052     EISSN: 17529867     Source Type: Journal    
DOI: 10.1093/mp/sst137     Document Type: Article
Times cited : (39)

References (59)
  • 1
    • 79952831697 scopus 로고    scopus 로고
    • The evolution of glycogen and starch metabolism in eukaryotes gives molecular clues to understand the establishment of plastid endosymbiosis
    • Ball, S., Colleoni, C., Cenci, U., Raj, J.N., and Tirtiaux, C. (2011). The evolution of glycogen and starch metabolism in eukaryotes gives molecular clues to understand the establishment of plastid endosymbiosis. J. Exp. Bot. 62, 1775-1801.
    • (2011) J. Exp. Bot. , vol.62 , pp. 1775-1801
    • Ball, S.1    Colleoni, C.2    Cenci, U.3    Raj, J.N.4    Tirtiaux, C.5
  • 2
    • 0142040430 scopus 로고    scopus 로고
    • From bacterial glycogen to starch: Understanding the biogenesis of the plant starch granule
    • Ball, S.G., and Morell, M.K. (2003). From bacterial glycogen to starch: understanding the biogenesis of the plant starch granule. Annu. Rev. Plant Biol. 54, 207-233.
    • (2003) Annu. Rev. Plant Biol. , vol.54 , pp. 207-233
    • Ball, S.G.1    Morell, M.K.2
  • 3
    • 0038653402 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis
    • Ballicora, M.A., Iglesias, A.A., and Preiss, J. (2003). ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis. Microbiol. Mol. Biol. Rev. 67, 213-225.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 213-225
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 4
    • 0442314288 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase: A regulatory enzyme for plant starch synthesis
    • Ballicora, M.A., Iglesias, A.A., and Preiss, J. (2004). ADP-glucose pyrophosphorylase: a regulatory enzyme for plant starch synthesis. Photosynth. Res. 79, 1-24.
    • (2004) Photosynth. Res. , vol.79 , pp. 1-24
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 5
    • 0032031956 scopus 로고    scopus 로고
    • The origin and evolution of oxygenic photosynthesis
    • Blankenship, R.E., and Hartman, H. (1998). The origin and evolution of oxygenic photosynthesis. Trends Biochem. Sci. 23, 94-97.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 94-97
    • Blankenship, R.E.1    Hartman, H.2
  • 6
    • 20044367629 scopus 로고    scopus 로고
    • Redox regulation: A broadening horizon
    • Buchanan, B.B., and Balmer, Y. (2005). Redox regulation: a broadening horizon. Annu. Rev. Plant Biol. 56, 187-220.
    • (2005) Annu. Rev. Plant Biol. , vol.56 , pp. 187-220
    • Buchanan, B.B.1    Balmer, Y.2
  • 7
    • 84867627581 scopus 로고    scopus 로고
    • Photo-catalytic conversion of carbon dioxide to organic acids by a recombinant cyanobacterium incapable of glycogen storage
    • Carrieri, D., Paddock, T., Maness, P.C., Seibert, M., and Yu, J. (2012). Photo-catalytic conversion of carbon dioxide to organic acids by a recombinant cyanobacterium incapable of glycogen storage. Energy Environ. Sci. 5, 9457-9461.
    • (2012) Energy Environ. Sci. , vol.5 , pp. 9457-9461
    • Carrieri, D.1    Paddock, T.2    Maness, P.C.3    Seibert, M.4    Yu, J.5
  • 8
    • 0043210400 scopus 로고    scopus 로고
    • The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme
    • Crevillen, P., Ballicora, M.A., Merida, A., Preiss, J., and Romero, J.M. (2003). The different large subunit isoforms of Arabidopsis thaliana ADP-glucose pyrophosphorylase confer distinct kinetic and regulatory properties to the heterotetrameric enzyme. J. Biol. Chem. 278, 28508-28515.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28508-28515
    • Crevillen, P.1    Ballicora, M.A.2    Merida, A.3    Preiss, J.4    Romero, J.M.5
  • 9
    • 80155142141 scopus 로고    scopus 로고
    • Large-scale phylogenomic analyses indicate a deep origin of primary plastids within cyanobacteria
    • Criscuolo, A., and Gribaldo, S. (2011). Large-scale phylogenomic analyses indicate a deep origin of primary plastids within cyanobacteria. Mol. Biol. Evol. 28, 3019-3032.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 3019-3032
    • Criscuolo, A.1    Gribaldo, S.2
  • 12
    • 0032566715 scopus 로고    scopus 로고
    • Mechanism of reductive activation of potato tuber ADP-glucose pyrophosphorylase
    • Fu, Y., Ballicora, M.A., Leykam, J.F., and Preiss, J. (1998). Mechanism of reductive activation of potato tuber ADP-glucose pyrophosphorylase. J. Biol. Chem. 273, 25045-25052.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25045-25052
    • Fu, Y.1    Ballicora, M.A.2    Leykam, J.F.3    Preiss, J.4
  • 14
    • 0034058881 scopus 로고    scopus 로고
    • NtcA represses transcription of gifA and gifB, genes that encode inhibitors of glutamine synthetase type i from Synechocystis sp. PCC 6803
    • Garcia-Dominguez, M., Reyes, J.C., and Florencio, F.J. (2000). NtcA represses transcription of gifA and gifB, genes that encode inhibitors of glutamine synthetase type I from Synechocystis sp. PCC 6803. Mol. Microbiol. 35, 1192-1201.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1192-1201
    • Garcia-Dominguez, M.1    Reyes, J.C.2    Florencio, F.J.3
  • 15
    • 43049177432 scopus 로고    scopus 로고
    • Molecular ecology and encironmental genomics of cyanobacteria
    • Genomics and Evolution, Herrero, A., and Flores, E., eds (Norfolk, UK: Caister Academic Press)
    • García-Pichel, F. (2008). Molecular ecology and encironmental genomics of cyanobacteria. In The Cyanobacteria: Molecular Biology, Genomics and Evolution, Herrero, A., and Flores, E., eds (Norfolk, UK: Caister Academic Press), pp. 59-88.
    • (2008) The Cyanobacteria: Molecular Biology , pp. 59-88
    • García-Pichel, F.1
  • 16
    • 84870344980 scopus 로고    scopus 로고
    • Impaired glycogen synthesis causes metabolic overflow reactions and affects stress responses in the cyanobacterium Synechocystis sp. PCC 6803
    • Grundel, M., Scheunemann, R., Lockau, W., and Zilliges, Y. (2012). Impaired glycogen synthesis causes metabolic overflow reactions and affects stress responses in the cyanobacterium Synechocystis sp. PCC 6803. Microbiology. 158, 3032-3043.
    • (2012) Microbiology. , vol.158 , pp. 3032-3043
    • Grundel, M.1    Scheunemann, R.2    Lockau, W.3    Zilliges, Y.4
  • 17
    • 84859510233 scopus 로고    scopus 로고
    • Mutagenesis of cysteine 81 prevents dimerization of the APS1 subunit of ADP-glucose pyrophosphorylase and alters diurnal starch turnover in Arabidopsis thaliana leaves
    • Hadrich, N., Hendriks, J.H., Kotting, O., Arrivault, S., Feil, R., Zeeman, S.C., Gibon, Y., Schulze, W.X., Stitt, M., and Lunn, J.E. (2012). Mutagenesis of cysteine 81 prevents dimerization of the APS1 subunit of ADP-glucose pyrophosphorylase and alters diurnal starch turnover in Arabidopsis thaliana leaves. Plant J. 70, 231-242.
    • (2012) Plant J. , vol.70 , pp. 231-242
    • Hadrich, N.1    Hendriks, J.H.2    Kotting, O.3    Arrivault, S.4    Feil, R.5    Zeeman, S.C.6    Gibon, Y.7    Schulze, W.X.8    Stitt, M.9    Lunn, J.E.10
  • 18
    • 0142214642 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase is activated by posttranslational redox-modification in response to light and to sugars in leaves of Arabidopsis and other plant species
    • Hendriks, J.H., Kolbe, A., Gibon, Y., Stitt, M., and Geigenberger, P. (2003). ADP-glucose pyrophosphorylase is activated by posttranslational redox-modification in response to light and to sugars in leaves of Arabidopsis and other plant species. Plant Physiol. 133, 838-849.
    • (2003) Plant Physiol. , vol.133 , pp. 838-849
    • Hendriks, J.H.1    Kolbe, A.2    Gibon, Y.3    Stitt, M.4    Geigenberger, P.5
  • 20
    • 63549116698 scopus 로고    scopus 로고
    • Proteins from multiple metabolic pathways associate with starch biosynthetic enzymes in high molecular weight complexes: A model for regulation of carbon allocation in maize amyloplasts
    • Hennen-Bierwagen, T.A., Lin, Q., Grimaud, F., Planchot, V., Keeling, P.L., James, M.G., and Myers, A.M. (2009). Proteins from multiple metabolic pathways associate with starch biosynthetic enzymes in high molecular weight complexes: a model for regulation of carbon allocation in maize amyloplasts. Plant Physiol. 149, 1541-1559.
    • (2009) Plant Physiol. , vol.149 , pp. 1541-1559
    • Hennen-Bierwagen, T.A.1    Lin, Q.2    Grimaud, F.3    Planchot, V.4    Keeling, P.L.5    James, M.G.6    Myers, A.M.7
  • 21
    • 5344241256 scopus 로고    scopus 로고
    • Rapid purification of the potato ADP-glucose pyrophosphorylase by polyhistidine-mediated chromatography
    • Hwang, S.K., Salamone, P.R., Kavakli, H., Slattery, C.J., and Okita, T.W. (2004). Rapid purification of the potato ADP-glucose pyrophosphorylase by polyhistidine-mediated chromatography. Protein Expr. Purif. 38, 99-107.
    • (2004) Protein Expr. Purif. , vol.38 , pp. 99-107
    • Hwang, S.K.1    Salamone, P.R.2    Kavakli, H.3    Slattery, C.J.4    Okita, T.W.5
  • 22
    • 33646241785 scopus 로고    scopus 로고
    • Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase
    • Iglesias, A.A., Ballicora, M.A., Sesma, J.I., and Preiss, J. (2006). Domain swapping between a cyanobacterial and a plant subunit ADP-glucose pyrophosphorylase. Plant Cell Physiol. 47, 523-530.
    • (2006) Plant Cell Physiol. , vol.47 , pp. 523-530
    • Iglesias, A.A.1    Ballicora, M.A.2    Sesma, J.I.3    Preiss, J.4
  • 23
    • 0000349941 scopus 로고
    • Regulatory and structural properties of the cyanobacterial ADPglucose pyrophosphorylases
    • Iglesias, A.A., Kakefuda, G., and Preiss, J. (1991). Regulatory and structural properties of the cyanobacterial ADPglucose pyrophosphorylases. Plant Physiol. 97, 1187-1195.
    • (1991) Plant Physiol. , vol.97 , pp. 1187-1195
    • Iglesias, A.A.1    Kakefuda, G.2    Preiss, J.3
  • 24
    • 15444377849 scopus 로고    scopus 로고
    • Crystal structure of potato tuber ADP-glucose pyrophosphorylase
    • Jin, X., Ballicora, M.A., Preiss, J., and Geiger, J.H. (2005). Crystal structure of potato tuber ADP-glucose pyrophosphorylase. EMBO J. 24, 694-704.
    • (2005) EMBO J. , vol.24 , pp. 694-704
    • Jin, X.1    Ballicora, M.A.2    Preiss, J.3    Geiger, J.H.4
  • 25
    • 79952078237 scopus 로고    scopus 로고
    • Compatible solute biosynthesis in cyanobacteria
    • Klahn, S., and Hagemann, M. (2011). Compatible solute biosynthesis in cyanobacteria. Environ. Microbiol. 13, 551-562.
    • (2011) Environ. Microbiol. , vol.13 , pp. 551-562
    • Klahn, S.1    Hagemann, M.2
  • 27
    • 84863143777 scopus 로고    scopus 로고
    • Post-translational redox modification of ADPglucose pyrophosphorylase in response to light is not a major determinant of fine regulation of transitory starch accumulation in Arabidopsis leaves
    • Li, J., et al. (2012). Post-translational redox modification of ADPglucose pyrophosphorylase in response to light is not a major determinant of fine regulation of transitory starch accumulation in Arabidopsis leaves. Plant Cell Physiol. 53, 433-444.
    • (2012) Plant Cell Physiol. , vol.53 , pp. 433-444
    • Li, J.1
  • 28
    • 33846845957 scopus 로고    scopus 로고
    • Identification of novel targets of cyanobacterial glutaredoxin
    • Li, M., Yang, Q., Zhang, L., Li, H., Cui, Y., and Wu, Q. (2007). Identification of novel targets of cyanobacterial glutaredoxin. Arch. Biochem. Biophys. 458, 220-228.
    • (2007) Arch. Biochem. Biophys. , vol.458 , pp. 220-228
    • Li, M.1    Yang, Q.2    Zhang, L.3    Li, H.4    Cui, Y.5    Wu, Q.6
  • 29
    • 0346103649 scopus 로고    scopus 로고
    • Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different
    • Lindahl, M., and Florencio, F.J. (2003). Thioredoxin-linked processes in cyanobacteria are as numerous as in chloroplasts, but targets are different. Proc. Natl Acad. Sci. U S A. 100, 16107-16112.
    • (2003) Proc. Natl Acad. Sci. U S A. , vol.100 , pp. 16107-16112
    • Lindahl, M.1    Florencio, F.J.2
  • 30
    • 1242271986 scopus 로고    scopus 로고
    • Systematic screening of reactive cysteine proteomes
    • Lindahl, M., and Florencio, F.J. (2004). Systematic screening of reactive cysteine proteomes. Proteomics. 4, 448-450.
    • (2004) Proteomics. , vol.4 , pp. 448-450
    • Lindahl, M.1    Florencio, F.J.2
  • 31
    • 84867640076 scopus 로고    scopus 로고
    • Cyanobacterial biofuel production
    • Machado, I.M., and Atsumi, S. (2012). Cyanobacterial biofuel production. J. Biotechnol. 162, 50-56.
    • (2012) J. Biotechnol. , vol.162 , pp. 50-56
    • MacHado, I.M.1    Atsumi, S.2
  • 32
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell, M.A., Haas, S.M., Bieber, L.L., and Tolbert, N.E. (1978). A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal. Biochem. 87, 206-210.
    • (1978) Anal. Biochem. , vol.87 , pp. 206-210
    • Markwell, M.A.1    Haas, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 33
    • 36048943681 scopus 로고    scopus 로고
    • Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin
    • Mata-Cabana, A., Florencio, F.J., and Lindahl, M. (2007). Membrane proteins from the cyanobacterium Synechocystis sp. PCC 6803 interacting with thioredoxin. Proteomics. 7, 3953-3963.
    • (2007) Proteomics. , vol.7 , pp. 3953-3963
    • Mata-Cabana, A.1    Florencio, F.J.2    Lindahl, M.3
  • 34
    • 0037339495 scopus 로고    scopus 로고
    • Changes in photosynthesis and pigmentation in an AGP deletion mutant of the cyanobacterium Synechocystis sp
    • Miao, X., Wu, Q., Wu, G., and Zhao, N. (2003). Changes in photosynthesis and pigmentation in an AGP deletion mutant of the cyanobacterium Synechocystis sp. Biotechnol. Lett. 25, 391-396.
    • (2003) Biotechnol. Lett. , vol.25 , pp. 391-396
    • Miao, X.1    Wu, Q.2    Wu, G.3    Zhao, N.4
  • 37
    • 0030221380 scopus 로고    scopus 로고
    • The cyanobacterial thioredoxin gene is required for both photoautotrophic and heterotrophic growth
    • Navarro, F., and Florencio, F.J. (1996). The cyanobacterial thioredoxin gene is required for both photoautotrophic and heterotrophic growth. Plant Physiol. 111, 1067-1075.
    • (1996) Plant Physiol. , vol.111 , pp. 1067-1075
    • Navarro, F.1    Florencio, F.J.2
  • 38
    • 17144472877 scopus 로고    scopus 로고
    • Electron transport controls transcription of the thioredoxin gene (trxA) in the cyanobacterium Synechocystis sp. PCC 6803
    • Navarro, F., Martin-Figueroa, E., and Florencio, F.J. (2000). Electron transport controls transcription of the thioredoxin gene (trxA) in the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol. Biol. 43, 23-32.
    • (2000) Plant Mol. Biol. , vol.43 , pp. 23-32
    • Navarro, F.1    Martin-Figueroa, E.2    Florencio, F.J.3
  • 39
    • 24744461378 scopus 로고    scopus 로고
    • Positive regulation of sugar catabolic pathways in the cyanobacterium Synechocystis sp. PCC 6803 by the group 2 sigma factor sigE
    • Osanai, T., Kanesaki, Y., Nakano, T., Takahashi, H., Asayama, M., Shirai, M., Kanehisa, M., Suzuki, I., Murata, N., and Tanaka, K. (2005). Positive regulation of sugar catabolic pathways in the cyanobacterium Synechocystis sp. PCC 6803 by the group 2 sigma factor sigE. J. Biol. Chem. 280, 30653-30659.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30653-30659
    • Osanai, T.1    Kanesaki, Y.2    Nakano, T.3    Takahashi, H.4    Asayama, M.5    Shirai, M.6    Kanehisa, M.7    Suzuki, I.8    Murata, N.9    Tanaka, K.10
  • 40
    • 33845866349 scopus 로고    scopus 로고
    • Nitrogen induction of sugar catabolic gene expression in Synechocystis sp. PCC 6803
    • Osanai, T., Imamura, S., Asayama, M., Shirai, M., Suzuki, I., Murata, N., and Tanaka, K. (2006). Nitrogen induction of sugar catabolic gene expression in Synechocystis sp. PCC 6803. DNA Res. 13, 185-195.
    • (2006) DNA Res. , vol.13 , pp. 185-195
    • Osanai, T.1    Imamura, S.2    Asayama, M.3    Shirai, M.4    Suzuki, I.5    Murata, N.6    Tanaka, K.7
  • 41
    • 68149102969 scopus 로고    scopus 로고
    • Complexity of cyanobacterial exopolysaccharides: Composition, structures, inducing factors and putative genes involved in their biosynthesis and assembly
    • Pereira, S., Zille, A., Micheletti, E., Moradas-Ferreira, P., De Philippis, R., and Tamagnini, P. (2009). Complexity of cyanobacterial exopolysaccharides: composition, structures, inducing factors and putative genes involved in their biosynthesis and assembly. FEMS Microbiol. Rev. 33, 917-941.
    • (2009) FEMS Microbiol. Rev. , vol.33 , pp. 917-941
    • Pereira, S.1    Zille, A.2    Micheletti, E.3    Moradas-Ferreira, P.4    De Philippis, R.5    Tamagnini, P.6
  • 42
    • 65249101414 scopus 로고    scopus 로고
    • Photosynthetic regulation of the cyanobacterium Synechocystis sp. PCC 6803 thioredoxin system and functional analysis of TrxB (Trx x) and TrxQ (Trx y) thioredoxins
    • Perez-Perez, M.E., Martin-Figueroa, E., and Florencio, F.J. (2009a). Photosynthetic regulation of the cyanobacterium Synechocystis sp. PCC 6803 thioredoxin system and functional analysis of TrxB (Trx x) and TrxQ (Trx y) thioredoxins. Mol. Plant. 2, 270-283.
    • (2009) Mol. Plant. , vol.2 , pp. 270-283
    • Perez-Perez, M.E.1    Martin-Figueroa, E.2    Florencio, F.J.3
  • 43
    • 72449202807 scopus 로고    scopus 로고
    • A comprehensive analysis of the peroxiredoxin reduction system in the Cyanobacterium Synechocystis sp. Strain PCC 6803 reveals that all five peroxiredoxins are thioredoxin dependent
    • Perez-Perez, M.E., Mata-Cabana, A., Sanchez-Riego, A.M., Lindahl, M., and Florencio, F.J. (2009b). A comprehensive analysis of the peroxiredoxin reduction system in the Cyanobacterium Synechocystis sp. strain PCC 6803 reveals that all five peroxiredoxins are thioredoxin dependent. J. Bacteriol. 191, 7477-7489.
    • (2009) J. Bacteriol. , vol.191 , pp. 7477-7489
    • Perez-Perez, M.E.1    Mata-Cabana, A.2    Sanchez-Riego, A.M.3    Lindahl, M.4    Florencio, F.J.5
  • 45
    • 0018409915 scopus 로고
    • Generic assignment, strain histories and properties of pure cultures of cyanobacteria
    • Rippka, R., Deruelles, J., Waterbury, J.B., Herman, M., and Stanier, R.Y. (1979). Generic assignment, strain histories and properties of pure cultures of cyanobacteria. J. Gen. Microbiol. 111, 1-61.
    • (1979) J. Gen. Microbiol. , vol.111 , pp. 1-61
    • Rippka, R.1    Deruelles, J.2    Waterbury, J.B.3    Herman, M.4    Stanier, R.Y.5
  • 46
  • 47
    • 84878018743 scopus 로고    scopus 로고
    • Overexpression of plastidial thioredoxin f leads to enhanced starch accumulation in tobacco leaves
    • Sanz-Barrio, R., Corral-Martinez, P., Ancin, M., Segui-Simarro, J.M., and Farran, I. (2013). Overexpression of plastidial thioredoxin f leads to enhanced starch accumulation in tobacco leaves. Plant Biotechnol. J. 11, 618-627.
    • (2013) Plant Biotechnol. J. , vol.11 , pp. 618-627
    • Sanz-Barrio, R.1    Corral-Martinez, P.2    Ancin, M.3    Segui-Simarro, J.M.4    Farran, I.5
  • 48
    • 77955073512 scopus 로고    scopus 로고
    • Integrative analysis of large scale expression profiles reveals core transcriptional response and coordination between multiple cellular processes in a cyanobacterium
    • Singh, A.K., Elvitigala, T., Cameron, J.C., Ghosh, B.K., Bhattacharyya-Pakrasi, M., and Pakrasi, H.B. (2010). Integrative analysis of large scale expression profiles reveals core transcriptional response and coordination between multiple cellular processes in a cyanobacterium. BMC Syst. Biol. 4, 105.
    • (2010) BMC Syst. Biol. , vol.4 , pp. 105
    • Singh, A.K.1    Elvitigala, T.2    Cameron, J.C.3    Ghosh, B.K.4    Bhattacharyya-Pakrasi, M.5    Pakrasi, H.B.6
  • 49
    • 84859358212 scopus 로고    scopus 로고
    • Modelling cyanobacteria: From metabolism to integrative models of phototrophic growth
    • Steuer, R., Knoop, H., and Machne, R. (2012). Modelling cyanobacteria: from metabolism to integrative models of phototrophic growth. J. Exp. Bot. 63, 2259-2274.
    • (2012) J. Exp. Bot. , vol.63 , pp. 2259-2274
    • Steuer, R.1    Knoop, H.2    MacHne, R.3
  • 51
    • 84875972010 scopus 로고    scopus 로고
    • Physicochemical variation of cyanobacterial starch, the insoluble alpha-glucans in cyanobacteria
    • Suzuki, E., Onoda, M., Colleoni, C., Ball, S., Fujita, N., and Nakamura, Y. (2013). Physicochemical variation of cyanobacterial starch, the insoluble alpha-glucans in cyanobacteria. Plant Cell Physiol. 54, 465-473.
    • (2013) Plant Cell Physiol. , vol.54 , pp. 465-473
    • Suzuki, E.1    Onoda, M.2    Colleoni, C.3    Ball, S.4    Fujita, N.5    Nakamura, Y.6
  • 52
    • 0038396066 scopus 로고    scopus 로고
    • Oscillation of mRNA level and activity of granule-bound starch synthase i in Arabidopsis leaves during the day/night cycle
    • Tenorio, G., Orea, A., Romero, J.M., and Merida, A. (2003). Oscillation of mRNA level and activity of granule-bound starch synthase I in Arabidopsis leaves during the day/night cycle. Plant Mol. Biol. 51, 949-958.
    • (2003) Plant Mol. Biol. , vol.51 , pp. 949-958
    • Tenorio, G.1    Orea, A.2    Romero, J.M.3    Merida, A.4
  • 54
    • 84875991056 scopus 로고    scopus 로고
    • Redox control of the activity of phosphoglycerate kinase in Synechocystis sp. PCC6803
    • Tsukamoto, Y., Fukushima, Y., Hara, S., and Hisabori, T. (2013). Redox control of the activity of phosphoglycerate kinase in Synechocystis sp. PCC6803. Plant Cell Physiol. 54, 484-491.
    • (2013) Plant Cell Physiol. , vol.54 , pp. 484-491
    • Tsukamoto, Y.1    Fukushima, Y.2    Hara, S.3    Hisabori, T.4
  • 56
    • 84864077086 scopus 로고    scopus 로고
    • Temporal orchestration of glycogen synthase (GlgA) gene expression and glycogen accumulation in the oceanic picoplanktonic cyanobacterium Synechococcus sp. Strain WH8103
    • Wyman, M., and Thom, C. (2012). Temporal orchestration of glycogen synthase (GlgA) gene expression and glycogen accumulation in the oceanic picoplanktonic cyanobacterium Synechococcus sp. strain WH8103. Appl. Environ. Microbiol. 78, 4744-4747.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 4744-4747
    • Wyman, M.1    Thom, C.2
  • 57
    • 84872420422 scopus 로고    scopus 로고
    • Altered carbohydrate metabolism in glycogen synthase mutants of Synechococcus sp. Strain PCC 7002: Cell factories for soluble sugars
    • Xu, Y., Tiago Guerra, L., Li, Z., Ludwig, M., Charles Dismukes, G., and Bryant, D.A. (2013). Altered carbohydrate metabolism in glycogen synthase mutants of Synechococcus sp. strain PCC 7002: cell factories for soluble sugars. Metab. Eng. 16C, 56-67.
    • (2013) Metab. Eng. , vol.16 C , pp. 56-67
    • Xu, Y.1    Tiago Guerra, L.2    Li, Z.3    Ludwig, M.4    Charles Dismukes, G.5    Bryant, D.A.6
  • 58
    • 0037137197 scopus 로고    scopus 로고
    • Characterization of cyanobacterial glycogen isolated from the wild type and from a mutant lacking of branching enzyme
    • Yoo, S.H., Spalding, M.H., and Jane, J.L. (2002). Characterization of cyanobacterial glycogen isolated from the wild type and from a mutant lacking of branching enzyme. Carbohydr. Res. 337, 2195-2203.
    • (2002) Carbohydr. Res. , vol.337 , pp. 2195-2203
    • Yoo, S.H.1    Spalding, M.H.2    Jane, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.