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Volumn 235, Issue 4, 2012, Pages 851-861

Sucrose phosphate phosphatase in the green alga Klebsormidium flaccidum (Streptophyta) lacks an extensive C-terminal domain and differs from that of land plants

Author keywords

C terminal domain; Green algae; Klebsormidium flaccidum; Streptophyta; Sucrose phosphate phosphatase; Sucrose synthesis

Indexed keywords

PHOSPHATASE; PHYTOHORMONE; SUCROSE; SUCROSE PHOSPHATASE; SUCROSE-PHOSPHATASE;

EID: 84858861390     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-011-1550-5     Document Type: Article
Times cited : (11)

References (53)
  • 1
    • 0023394634 scopus 로고
    • Modes of interaction of cryoprotectants with membrane phospholipids during freezing
    • Anchordoguy TJ, Rudolph AS, Carpenter JF, Crowe JH (1987) Modes of interaction of cryoprotectants with membrane phospholipids during freezing. Cryobiology 24: 324-331.
    • (1987) Cryobiology , vol.24 , pp. 324-331
    • Anchordoguy, T.J.1    Rudolph, A.S.2    Carpenter, J.F.3    Crowe, J.H.4
  • 2
    • 0031970010 scopus 로고    scopus 로고
    • The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold
    • Aravind L, Galperin MY, Koonin EV (1998) The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Trends Biochem Sci 23: 127-129.
    • (1998) Trends Biochem Sci , vol.23 , pp. 127-129
    • Aravind, L.1    Galperin, M.Y.2    Koonin, E.V.3
  • 3
    • 0031758603 scopus 로고    scopus 로고
    • Algal phylogeny and the origin of land plants
    • Bhattacharya D, Medlin L (1998) Algal phylogeny and the origin of land plants. Plant Physiol 116: 9-15.
    • (1998) Plant Physiol , vol.116 , pp. 9-15
    • Bhattacharya, D.1    Medlin, L.2
  • 5
    • 36749012490 scopus 로고    scopus 로고
    • RNA interference-mediated repression of sucrose-phosphatase in transgenic potato tubers (Solanum tuberosum) strongly affects the hexose-to-sucrose ratio upon cold storage with only minor effects on total soluble carbohydrate accumulation
    • Chen S, Hajirezaei MR, Zanor M-I, Hornyik C, Debast S, Lacomme C, Ferine AR, Sonnewald U, Börnke F (2007) RNA interference-mediated repression of sucrose-phosphatase in transgenic potato tubers (Solanum tuberosum) strongly affects the hexose-to-sucrose ratio upon cold storage with only minor effects on total soluble carbohydrate accumulation. Plant Cell Environ 31: 165-176.
    • (2007) Plant Cell Environ , vol.31 , pp. 165-176
    • Chen, S.1    Hajirezaei, M.R.2    Zanor, M.-I.3    Hornyik, C.4    Debast, S.5    Lacomme, C.6    Ferine, A.R.7    Sonnewald, U.8    Börnke, F.9
  • 6
    • 0032486282 scopus 로고    scopus 로고
    • A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif
    • Collet JF, Stroobant V, Pirard M, Delpierre G, van Schaftingen E (1998) A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif. J Biol Chem 23: 14107-14112.
    • (1998) J Biol Chem , vol.23 , pp. 14107-14112
    • Collet, J.F.1    Stroobant, V.2    Pirard, M.3    Delpierre, G.4    van Schaftingen, E.5
  • 7
    • 0037165644 scopus 로고    scopus 로고
    • Sucrose metabolism: Anabaena sucrose-phosphate synthase and sucrose-phosphate phosphatase define minimal functional domains shuffled during evolution
    • Cumino A, Curatti L, Giarrocco L, Salerno GL (2002) Sucrose metabolism: Anabaena sucrose-phosphate synthase and sucrose-phosphate phosphatase define minimal functional domains shuffled during evolution. FEBS Lett 517: 19-23.
    • (2002) FEBS Lett , vol.517 , pp. 19-23
    • Cumino, A.1    Curatti, L.2    Giarrocco, L.3    Salerno, G.L.4
  • 8
    • 78249271725 scopus 로고    scopus 로고
    • The proteins involved in sucrose synthesis in the marine cyanobacterium Synechococcus sp. PCC 7002 are encoded by two genes transcribed from a gene cluster
    • Cumino A, Perez-Cenci M, Giarrocco L, Salerno GL (2010) The proteins involved in sucrose synthesis in the marine cyanobacterium Synechococcus sp. PCC 7002 are encoded by two genes transcribed from a gene cluster. FEBS Lett 584: 4655-4660.
    • (2010) FEBS Lett , vol.584 , pp. 4655-4660
    • Cumino, A.1    Perez-Cenci, M.2    Giarrocco, L.3    Salerno, G.L.4
  • 9
    • 0017391366 scopus 로고
    • Sucrose metabolism in green algae I. The presence of sucrose synthase and sucrose phosphate synthase
    • Duran WR, Pontis HG (1977) Sucrose metabolism in green algae I. The presence of sucrose synthase and sucrose phosphate synthase. Mol Cell Biochem 16: 149-152.
    • (1977) Mol Cell Biochem , vol.16 , pp. 149-152
    • Duran, W.R.1    Pontis, H.G.2
  • 10
    • 0031403569 scopus 로고    scopus 로고
    • Physical and kinetic evidence for an association between sucrose phosphate synthase and sucrose-phosphate phosphatase
    • Echeverria E, Salvucci ME, Gonzalez P, Paris P, Salerno G (1997) Physical and kinetic evidence for an association between sucrose phosphate synthase and sucrose-phosphate phosphatase. Plant Physiol 115: 223-227.
    • (1997) Plant Physiol , vol.115 , pp. 223-227
    • Echeverria, E.1    Salvucci, M.E.2    Gonzalez, P.3    Paris, P.4    Salerno, G.5
  • 11
    • 57349149050 scopus 로고    scopus 로고
    • Freezing and desiccation injury resistance in the filamentous green alga Klebsormidium from the Antarctic, Arctic and Slovakia
    • Elster J, Degma P, Kovacik L, Valentova L, Sramkova K, Pereira AB (2008) Freezing and desiccation injury resistance in the filamentous green alga Klebsormidium from the Antarctic, Arctic and Slovakia. Biologia 63: 843-851.
    • (2008) Biologia , vol.63 , pp. 843-851
    • Elster, J.1    Degma, P.2    Kovacik, L.3    Valentova, L.4    Sramkova, K.5    Pereira, A.B.6
  • 12
    • 33644798734 scopus 로고    scopus 로고
    • The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell
    • Fieulaine S, Lunn JE, Borel F, Ferrer JL (2005) The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell. Plant Cell 17: 2049-2058.
    • (2005) Plant Cell , vol.17 , pp. 2049-2058
    • Fieulaine, S.1    Lunn, J.E.2    Borel, F.3    Ferrer, J.L.4
  • 13
    • 0034712758 scopus 로고    scopus 로고
    • The origin of plants: body plan changes contributing to a major evolutionary radiation
    • Graham LE, Cook ME, Busse JS (2000) The origin of plants: body plan changes contributing to a major evolutionary radiation. Proc Natl Acad Sci USA 97: 4535-4540.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4535-4540
    • Graham, L.E.1    Cook, M.E.2    Busse, J.S.3
  • 14
    • 0001419897 scopus 로고
    • Sucrose phosphate synthase and sucrose accumulation at low temperature
    • Guy CL, Huber JL, Huber SC (1992) Sucrose phosphate synthase and sucrose accumulation at low temperature. Plant Physiol 100: 502-508.
    • (1992) Plant Physiol , vol.100 , pp. 502-508
    • Guy, C.L.1    Huber, J.L.2    Huber, S.C.3
  • 15
    • 0342349041 scopus 로고
    • Enzymes concerned with sucrose synthesis and transformations in seeds of maize, broad bean and castor bean
    • Hawker JS (1971) Enzymes concerned with sucrose synthesis and transformations in seeds of maize, broad bean and castor bean. Phytochemistry 10: 2313-2322.
    • (1971) Phytochemistry , vol.10 , pp. 2313-2322
    • Hawker, J.S.1
  • 16
    • 0000760288 scopus 로고
    • Occurrence of sucrose phosphatase in vascular and non-vascular plants
    • Hawker JS, Smith GM (1984) Occurrence of sucrose phosphatase in vascular and non-vascular plants. Phytochemistry 23: 245-249.
    • (1984) Phytochemistry , vol.23 , pp. 245-249
    • Hawker, J.S.1    Smith, G.M.2
  • 17
    • 79958773208 scopus 로고    scopus 로고
    • Desiccation stress causes structural and ultrastructural alterations in the aeroterrestrial green alga Klebsormidium crenulatum (Klebsormidiophyceae, Streptophyta) isolated from an alpine soil crust
    • Holzinger A, Lutz C, Karsten U (2011) Desiccation stress causes structural and ultrastructural alterations in the aeroterrestrial green alga Klebsormidium crenulatum (Klebsormidiophyceae, Streptophyta) isolated from an alpine soil crust. J Phycol 47: 591-602.
    • (2011) J Phycol , vol.47 , pp. 591-602
    • Holzinger, A.1    Lutz, C.2    Karsten, U.3
  • 18
    • 0040419081 scopus 로고    scopus 로고
    • Role and regulation of sucrose-phosphate synthase in higher plants
    • Huber SC, Huber JL (1996) Role and regulation of sucrose-phosphate synthase in higher plants. Annu Rev Plant Physiol Plant Mol Biol 47: 431-444.
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 431-444
    • Huber, S.C.1    Huber, J.L.2
  • 20
    • 9344238199 scopus 로고    scopus 로고
    • Solute accumulation in wheat seedlings during cold acclimation: contribution to freezing tolerance
    • Kamata T, Uemura M (2004) Solute accumulation in wheat seedlings during cold acclimation: contribution to freezing tolerance. CryoLett 25: 311-322.
    • (2004) CryoLett , vol.25 , pp. 311-322
    • Kamata, T.1    Uemura, M.2
  • 21
    • 34250177304 scopus 로고    scopus 로고
    • Transcript and metabolite profiling during cold acclimation of Arabidopsis reveals an intricate relationship of cold-regulated gene expression with modifications in metabolite content
    • Kaplan F, Kopka J, Sung DY, Zhao W, Popp M, Porat R, Guy CL (2007) Transcript and metabolite profiling during cold acclimation of Arabidopsis reveals an intricate relationship of cold-regulated gene expression with modifications in metabolite content. Plant J 50: 967-981.
    • (2007) Plant J , vol.50 , pp. 967-981
    • Kaplan, F.1    Kopka, J.2    Sung, D.Y.3    Zhao, W.4    Popp, M.5    Porat, R.6    Guy, C.L.7
  • 23
    • 85016881453 scopus 로고    scopus 로고
    • Ecophysiological performance of an urban strain of the aeroterrestrial green alga Klebsormidium sp (Klebsormidiales, Klebsormidiophyceae)
    • Karsten U, Rindi F (2010) Ecophysiological performance of an urban strain of the aeroterrestrial green alga Klebsormidium sp (Klebsormidiales, Klebsormidiophyceae). Eur J Phycol 45: 426-435.
    • (2010) Eur J Phycol , vol.45 , pp. 426-435
    • Karsten, U.1    Rindi, F.2
  • 24
    • 78649896344 scopus 로고    scopus 로고
    • Ecophysiological performance of the aeroterrestrial green alga Klebsormidium crenulatum (Charophyceae, Streptophyta) isolated from an alpine soil crust with an emphasis on desiccation stress
    • Karsten U, Lutz C, Holzinger A (2010) Ecophysiological performance of the aeroterrestrial green alga Klebsormidium crenulatum (Charophyceae, Streptophyta) isolated from an alpine soil crust with an emphasis on desiccation stress. J Phycol 46: 1187-1197.
    • (2010) J Phycol , vol.46 , pp. 1187-1197
    • Karsten, U.1    Lutz, C.2    Holzinger, A.3
  • 25
    • 2442459991 scopus 로고    scopus 로고
    • Sucrose metabolism: regulatory mechanisms and pivotal roles in sugar sensing and polant development
    • Koch K (2004) Sucrose metabolism: regulatory mechanisms and pivotal roles in sugar sensing and polant development. Curr Opin Plant Biol 7: 235-246.
    • (2004) Curr Opin Plant Biol , vol.7 , pp. 235-246
    • Koch, K.1
  • 26
    • 77955874692 scopus 로고    scopus 로고
    • Sucrose transporters of higher plants
    • Kühn C, Grof CPL (2010) Sucrose transporters of higher plants. Curr Opin Plant Biol 13: 287-297.
    • (2010) Curr Opin Plant Biol , vol.13 , pp. 287-297
    • Kühn, C.1    Grof, C.P.L.2
  • 28
    • 0028838470 scopus 로고
    • Trehalose and sucrose protect both membranes and proteins in intact bacteria during drying
    • Leslie SB, Israeli E, Lighthart B, Crowe JH, Crowe LM (1995) Trehalose and sucrose protect both membranes and proteins in intact bacteria during drying. Appl Environ Microbiol 61: 3592-3597.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 3592-3597
    • Leslie, S.B.1    Israeli, E.2    Lighthart, B.3    Crowe, J.H.4    Crowe, L.M.5
  • 29
    • 0344896842 scopus 로고    scopus 로고
    • Phylogenetic affinities of the Trentepohliales inferred from small-subunit rDNA
    • López-Bautista JM, Chapman RL (2003) Phylogenetic affinities of the Trentepohliales inferred from small-subunit rDNA. Int J Syst Evol Microbiol 53: 2099-2106.
    • (2003) Int J Syst Evol Microbiol , vol.53 , pp. 2099-2106
    • López-Bautista, J.M.1    Chapman, R.L.2
  • 30
    • 0025271020 scopus 로고
    • Apparent equilibrium constant and mass-action ratio for sucrose-phosphate synthase in seeds of Pisum sativum
    • Lunn JE, ap Rees T (1990) Apparent equilibrium constant and mass-action ratio for sucrose-phosphate synthase in seeds of Pisum sativum. Biochem J 267: 739-743.
    • (1990) Biochem J , vol.267 , pp. 739-743
    • Lunn, J.E.1    Ap Rees, T.2
  • 32
    • 0030999095 scopus 로고    scopus 로고
    • The role of sucrose-phosphate synthase in the control of photosynthate partitioning in Zea mays leaves
    • Lunn JE, Hatch MD (1997) The role of sucrose-phosphate synthase in the control of photosynthate partitioning in Zea mays leaves. Aust J Plant Physiolo 24: 1-8.
    • (1997) Aust J Plant Physiolo , vol.24 , pp. 1-8
    • Lunn, J.E.1    Hatch, M.D.2
  • 33
    • 0033136352 scopus 로고    scopus 로고
    • Cloning and expression of a prokaryotic sucrose-phosphate synthase gene from the cyanobacterium Synechocystis sp. PCC 6803
    • Lunn JE, Price GD, Furbank RT (1999) Cloning and expression of a prokaryotic sucrose-phosphate synthase gene from the cyanobacterium Synechocystis sp. PCC 6803. Plant Mol Biol 40: 297-305.
    • (1999) Plant Mol Biol , vol.40 , pp. 297-305
    • Lunn, J.E.1    Price, G.D.2    Furbank, R.T.3
  • 35
    • 0036010499 scopus 로고    scopus 로고
    • Evolution of sucrose synthesis
    • Lunn JE (2002) Evolution of sucrose synthesis. Plant Physiol 128: 1490-1500.
    • (2002) Plant Physiol , vol.128 , pp. 1490-1500
    • Lunn, J.E.1
  • 36
    • 0037448604 scopus 로고    scopus 로고
    • Sucrose-phosphatase gene families in plants
    • Lunn JE (2003) Sucrose-phosphatase gene families in plants. Gene 303: 187-196.
    • (2003) Gene , vol.303 , pp. 187-196
    • Lunn, J.E.1
  • 37
    • 0038810298 scopus 로고    scopus 로고
    • New complexities in the synthesis of sucrose
    • Lunn JE, MacRae E (2003) New complexities in the synthesis of sucrose. Curr Opi Plant Biol 6: 208-214.
    • (2003) Curr Opi Plant Biol , vol.6 , pp. 208-214
    • Lunn, J.E.1    Macrae, E.2
  • 39
    • 0034730072 scopus 로고    scopus 로고
    • The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily
    • Morais MC, Zhang W, Baker AS, Zhang G, Dunaway-Mariano D, Allen KN (2000) The crystal structure of Bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. Biochemistry 39: 10385-10396.
    • (2000) Biochemistry , vol.39 , pp. 10385-10396
    • Morais, M.C.1    Zhang, W.2    Baker, A.S.3    Zhang, G.4    Dunaway-Mariano, D.5    Allen, K.N.6
  • 40
    • 33645102313 scopus 로고    scopus 로고
    • Accumulation of theanderose in association with development of freezing tolerance in the moss Physcomitrella patens
    • Nagao M, Oku K, Minami A, Mizuno K, Sakurai M, Arakawa K, Fujikawa S, Takezawa D (2006) Accumulation of theanderose in association with development of freezing tolerance in the moss Physcomitrella patens. Phytochemistry 67: 702-709.
    • (2006) Phytochemistry , vol.67 , pp. 702-709
    • Nagao, M.1    Oku, K.2    Minami, A.3    Mizuno, K.4    Sakurai, M.5    Arakawa, K.6    Fujikawa, S.7    Takezawa, D.8
  • 41
    • 43449140000 scopus 로고    scopus 로고
    • Klebsormidium flaccidum, a charophycean green alga, exhibits cold acclimation that is closely associated with compatible solute accumulation and ultrastructural changes
    • Nagao M, Matsui K, Uemura M (2008) Klebsormidium flaccidum, a charophycean green alga, exhibits cold acclimation that is closely associated with compatible solute accumulation and ultrastructural changes. Plant Cell Environ 31: 872-885.
    • (2008) Plant Cell Environ , vol.31 , pp. 872-885
    • Nagao, M.1    Matsui, K.2    Uemura, M.3
  • 43
    • 33646867843 scopus 로고    scopus 로고
    • The GapA/B Gene Duplication Marks the Origin of Streptophyta (Charophytes and Land Plants)
    • Petersen J, Teich R, Becker B, Cerff R, Brinkmann H (2007) The GapA/B Gene Duplication Marks the Origin of Streptophyta (Charophytes and Land Plants). Mol Biol Evol 23: 1109-1118.
    • (2007) Mol Biol Evol , vol.23 , pp. 1109-1118
    • Petersen, J.1    Teich, R.2    Becker, B.3    Cerff, R.4    Brinkmann, H.5
  • 44
    • 0040409833 scopus 로고
    • Occurrence of sucrose and sucrose metabolizing enzymes in achlorophyllous algae
    • Salerno GL (1985) Occurrence of sucrose and sucrose metabolizing enzymes in achlorophyllous algae. Plant Sci 42: 5-8.
    • (1985) Plant Sci , vol.42 , pp. 5-8
    • Salerno, G.L.1
  • 45
    • 0037937490 scopus 로고    scopus 로고
    • Origin of sucrose metabolism in higher plants: when, how and why?
    • Salerno GL, Curatti L (2003) Origin of sucrose metabolism in higher plants: when, how and why? Trends Plant Sci 8: 63-69.
    • (2003) Trends Plant Sci , vol.8 , pp. 63-69
    • Salerno, G.L.1    Curatti, L.2
  • 46
    • 0000348029 scopus 로고
    • The generic name Hormidium as applied to green algae
    • Silva PC, Mattox KR, Blackwell WH Jr (1972) The generic name Hormidium as applied to green algae. Taxon 21: 639-645.
    • (1972) Taxon , vol.21 , pp. 639-645
    • Silva, P.C.1    Mattox, K.R.2    Blackwell Jr., W.H.3
  • 47
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • doi: 10. 1093/molbev/msr121
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol doi: 10. 1093/molbev/msr121.
    • (2011) Mol Biol Evol
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 48
    • 0032161654 scopus 로고    scopus 로고
    • Role of cold-responsive genes in plant freezing tolerance
    • Thomashow MF (1998) Role of cold-responsive genes in plant freezing tolerance. Plant Physiol 118: 1-7.
    • (1998) Plant Physiol , vol.118 , pp. 1-7
    • Thomashow, M.F.1
  • 49
    • 77957748106 scopus 로고    scopus 로고
    • Molecular basis of plant cold acclimation: insights gained from studying the CBF cold response pathway
    • Thomashow MF (2010) Molecular basis of plant cold acclimation: insights gained from studying the CBF cold response pathway. Plant Physiol 154: 571-577.
    • (2010) Plant Physiol , vol.154 , pp. 571-577
    • Thomashow, M.F.1
  • 50
    • 0032508671 scopus 로고    scopus 로고
    • Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins
    • Toroser D, Athwal GS, Huber SC (1998) Site-specific regulatory interaction between spinach leaf sucrose-phosphate synthase and 14-3-3 proteins. FEBS Lett 435: 110-114.
    • (1998) FEBS Lett , vol.435 , pp. 110-114
    • Toroser, D.1    Athwal, G.S.2    Huber, S.C.3
  • 51
    • 0013060608 scopus 로고    scopus 로고
    • Modification of the intracellular sugar content alters the incident of freeze-induced membrane lesions of protoplasts isolated from Arabidopsis thaliana leaves
    • Uemura M, Steponkus PL (2003) Modification of the intracellular sugar content alters the incident of freeze-induced membrane lesions of protoplasts isolated from Arabidopsis thaliana leaves. Plant Cell Environ 26: 1083-1096.
    • (2003) Plant Cell Environ , vol.26 , pp. 1083-1096
    • Uemura, M.1    Steponkus, P.L.2
  • 52
    • 0344080484 scopus 로고    scopus 로고
    • Freezing sensitivity in the sfr4 mutant of Arabidopsis is due to low sugar content and is manifested by loss of osmotic responsiveness
    • Uemura M, Warren G, Steponkus PL (2003) Freezing sensitivity in the sfr4 mutant of Arabidopsis is due to low sugar content and is manifested by loss of osmotic responsiveness. Plant Physiol 131: 1800-1807.
    • (2003) Plant Physiol , vol.131 , pp. 1800-1807
    • Uemura, M.1    Warren, G.2    Steponkus, P.L.3
  • 53
    • 0035155638 scopus 로고    scopus 로고
    • Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1.8 Å resolution
    • Wang W, Kim R, Jancarik J, Yokota H, Kim SH (2001) Crystal structure of phosphoserine phosphatase from Methanococcus jannaschii, a hyperthermophile, at 1. 8 Å resolution. Structure 9: 65-71.
    • (2001) Structure , vol.9 , pp. 65-71
    • Wang, W.1    Kim, R.2    Jancarik, J.3    Yokota, H.4    Kim, S.H.5


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