메뉴 건너뛰기




Volumn 135, Issue 3, 2004, Pages 1674-1684

β-amylase induction and the protective role of maltose during temperature shock

Author keywords

[No Author keywords available]

Indexed keywords

BIOASSAY; BIODEGRADATION; ELECTRON TRANSPORT PROPERTIES; ENZYMES; GENES; MALTOSE; PHOTOSYNTHESIS; PLANTS (BOTANY); STARCH;

EID: 3543023347     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.104.040808     Document Type: Article
Times cited : (398)

References (42)
  • 2
  • 3
    • 84980184968 scopus 로고
    • The quantitative analysis of chlorophylls a and b in plant extracts
    • Bruinsma J (1963) The quantitative analysis of chlorophylls a and b in plant extracts. Photochem Photobiol 2: 241-249
    • (1963) Photochem Photobiol , vol.2 , pp. 241-249
    • Bruinsma, J.1
  • 4
    • 0034772892 scopus 로고    scopus 로고
    • A novel putative beta-amylase gene and Atb-Amy from Arabidopsis thaliana are circadian regulated
    • Chandler JW, Apel K, Melzer S (2001) A novel putative beta-amylase gene and Atb-Amy from Arabidopsis thaliana are circadian regulated. Plant Sci 161: 1019-1024
    • (2001) Plant Sci , vol.161 , pp. 1019-1024
    • Chandler, J.W.1    Apel, K.2    Melzer, S.3
  • 5
    • 0027494820 scopus 로고
    • Multiple pathways for protein transport into or across the thylakoid membrane
    • Cline K, Henry R, Li CJ, Yuan J (1993) Multiple pathways for protein transport into or across the thylakoid membrane. EMBO J 12: 4105-4114
    • (1993) EMBO J , vol.12 , pp. 4105-4114
    • Cline, K.1    Henry, R.2    Li, C.J.3    Yuan, J.4
  • 6
    • 0032869376 scopus 로고    scopus 로고
    • Stress-mediated enhancement of beta-amylase activity in pearl millet and maize leaves is dependent on light
    • Datta R, Selvi MT, Seetharama N, Sharma R (1999) Stress-mediated enhancement of beta-amylase activity in pearl millet and maize leaves is dependent on light. J Plant Physiol 154: 657-664
    • (1999) J Plant Physiol , vol.154 , pp. 657-664
    • Datta, R.1    Selvi, M.T.2    Seetharama, N.3    Sharma, R.4
  • 7
    • 0001085170 scopus 로고
    • Beta-amylases from alfalfa (Medicago sativa L.) roots
    • Doehlert DC, Duke SH, Anderson L (1982) Beta-amylases from alfalfa (Medicago sativa L.) roots. Plant Physiol 69: 1096-1102
    • (1982) Plant Physiol , vol.69 , pp. 1096-1102
    • Doehlert, D.C.1    Duke, S.H.2    Anderson, L.3
  • 8
    • 0029135828 scopus 로고
    • Light- and stress-dependent enhancement of amylolytic activities in white and green barley leaves: Beta-amylases are stress-induced proteins
    • Dreier W, Schnarrenberger C, Börner T (1995) Light- and stress-dependent enhancement of amylolytic activities in white and green barley leaves: beta-amylases are stress-induced proteins. J Plant Physiol 145: 342-348
    • (1995) J Plant Physiol , vol.145 , pp. 342-348
    • Dreier, W.1    Schnarrenberger, C.2    Börner, T.3
  • 9
    • 0036671216 scopus 로고    scopus 로고
    • Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway
    • Fowler S, Thomashow MF (2002) Arabidopsis transcriptome profiling indicates that multiple regulatory pathways are activated during cold acclimation in addition to the CBF cold response pathway. Plant Cell 14: 1675-1690
    • (2002) Plant Cell , vol.14 , pp. 1675-1690
    • Fowler, S.1    Thomashow, M.F.2
  • 11
    • 0000992348 scopus 로고
    • Conversion of free beta-amylase to bound beta-amylase on starch granules in the barley endosperm during desiccation phase of seed development
    • Hara-Nishimura I, Nishimura M, Daussant J (1986) Conversion of free beta-amylase to bound beta-amylase on starch granules in the barley endosperm during desiccation phase of seed development. Protoplasma 134: 149-153
    • (1986) Protoplasma , vol.134 , pp. 149-153
    • Hara-Nishimura, I.1    Nishimura, M.2    Daussant, J.3
  • 13
    • 0038019453 scopus 로고    scopus 로고
    • Use of SAGE technology to reveal changes in gene expression in Arabidopsis leaves undergoing cold stress
    • Jung S-H, Lee J-Y, Lee D-H (2003) Use of SAGE technology to reveal changes in gene expression in Arabidopsis leaves undergoing cold stress. Plant Mol Biol 52: 553-567
    • (2003) Plant Mol Biol , vol.52 , pp. 553-567
    • Jung, S.-H.1    Lee, J.-Y.2    Lee, D.-H.3
  • 14
    • 0033940474 scopus 로고    scopus 로고
    • Understanding and influencing starch biochemistry
    • Kossmann J, Lloyd J (2000) Understanding and influencing starch biochemistry. Crit Rev Biochem Mol Biol 35: 141-196
    • (2000) Crit Rev Biochem Mol Biol , vol.35 , pp. 141-196
    • Kossmann, J.1    Lloyd, J.2
  • 15
    • 0036909761 scopus 로고    scopus 로고
    • Transcriptome changes for Arabidopsis in response to salt osmotic and cold stress
    • Kreps JA, Wu Y, Chang SH, Zhu T, Wang X, Harper JF (2002) Transcriptome changes for Arabidopsis in response to salt osmotic and cold stress. Plant Physiol 130: 2129-2141
    • (2002) Plant Physiol , vol.130 , pp. 2129-2141
    • Kreps, J.A.1    Wu, Y.2    Chang, S.H.3    Zhu, T.4    Wang, X.5    Harper, J.F.6
  • 17
    • 3543037569 scopus 로고
    • Changes in metabolites of red-osier dogwood during cold acclimation
    • Li PH, Weiser CJ, van Huystee R (1965) Changes in metabolites of red-osier dogwood during cold acclimation. J Am Soc Hortic Sci 86: 723-730
    • (1965) J Am Soc Hortic Sci , vol.86 , pp. 723-730
    • Li, P.H.1    Weiser, C.J.2    Van Huystee, R.3
  • 18
    • 0000603887 scopus 로고
    • Purification and characterization of pea epicotyl beta-amylase
    • Lizotte PA, Henson CA, Duke SH (1990) Purification and characterization of pea epicotyl beta-amylase. Plant Physiol 92: 615-621
    • (1990) Plant Physiol , vol.92 , pp. 615-621
    • Lizotte, P.A.1    Henson, C.A.2    Duke, S.H.3
  • 19
    • 0742319992 scopus 로고    scopus 로고
    • The role of amylomaltase in maltose metabolism in the cytosol of photosynthetic cells
    • Lu Y, Sharkey TD (2004) The role of amylomaltase in maltose metabolism in the cytosol of photosynthetic cells. Planta 218: 466-473
    • (2004) Planta , vol.218 , pp. 466-473
    • Lu, Y.1    Sharkey, T.D.2
  • 21
    • 0029257520 scopus 로고
    • Sugar-inducible expression of a gene for beta-amylase in Arabidopsis thaliana
    • Mita S, Suzuki-Fujii K, Nakamura K (1995) Sugar-inducible expression of a gene for beta-amylase in Arabidopsis thaliana. Plant Physiol 107: 895-904
    • (1995) Plant Physiol , vol.107 , pp. 895-904
    • Mita, S.1    Suzuki-Fujii, K.2    Nakamura, K.3
  • 22
    • 0009466084 scopus 로고
    • Purification of a β-amylase that accumulates in Arabidopsis thaliana mutants defective in starch metabolism
    • Monroe JD, Preiss J (1990) Purification of a β-amylase that accumulates in Arabidopsis thaliana mutants defective in starch metabolism. Plant Physiol 94: 1033-1039
    • (1990) Plant Physiol , vol.94 , pp. 1033-1039
    • Monroe, J.D.1    Preiss, J.2
  • 23
    • 0001095351 scopus 로고
    • Sucrose-induced accumulation of beta-amylase occurs concomitant with the accumulation of starch and sporamin in leaf-petiole cuttings of sweet potato
    • Nakamura K, Ohto M, Yoshida N, Nakamura K (1991) Sucrose-induced accumulation of beta-amylase occurs concomitant with the accumulation of starch and sporamin in leaf-petiole cuttings of sweet potato. Plant Physiol 96: 902-909
    • (1991) Plant Physiol , vol.96 , pp. 902-909
    • Nakamura, K.1    Ohto, M.2    Yoshida, N.3    Nakamura, K.4
  • 24
    • 0030901647 scopus 로고    scopus 로고
    • A beta-amylase in potato tubers is induced by storage at low temperature
    • Nielsen TM, Deiting U, Stitt M (1997) A beta-amylase in potato tubers is induced by storage at low temperature. Plant Physiol 113: 503-510
    • (1997) Plant Physiol , vol.113 , pp. 503-510
    • Nielsen, T.M.1    Deiting, U.2    Stitt, M.3
  • 25
    • 0346096943 scopus 로고    scopus 로고
    • A previously unknown maltose transporter essential for starch degradation in leaves
    • Niittyla T, Messerli G, Trevisan M, Chen J, Smith AM, Zeeman SC (2004) A previously unknown maltose transporter essential for starch degradation in leaves. Science 303: 87-89
    • (2004) Science , vol.303 , pp. 87-89
    • Niittyla, T.1    Messerli, G.2    Trevisan, M.3    Chen, J.4    Smith, A.M.5    Zeeman, S.C.6
  • 26
    • 0001584686 scopus 로고
    • Induction of expression of genes coding for sporamin and beta-amylase by polygalacturonic acid in leaf-petiole cuttings of sweet potato
    • Ohto M-A, Nakamura-Kito K, Nakamura K (1992) Induction of expression of genes coding for sporamin and beta-amylase by polygalacturonic acid in leaf-petiole cuttings of sweet potato. Plant Physiol 99: 422-427
    • (1992) Plant Physiol , vol.99 , pp. 422-427
    • Ohto, M.-A.1    Nakamura-Kito, K.2    Nakamura, K.3
  • 27
    • 0033990117 scopus 로고    scopus 로고
    • Low cost gel analysis
    • Reidler JA (2000) Low cost gel analysis. Methods Mol Biol 132: 277-288
    • (2000) Methods Mol Biol , vol.132 , pp. 277-288
    • Reidler, J.A.1
  • 28
    • 6544290514 scopus 로고    scopus 로고
    • Metabolic engineering of rice leading to biosynthesis of glycine betaine to salt and cold
    • Sakamoto A, Alia, Murata N, Murata A (1998) Metabolic engineering of rice leading to biosynthesis of glycine betaine to salt and cold. Plant Mol Biol 38: 1011-1019
    • (1998) Plant Mol Biol , vol.38 , pp. 1011-1019
    • Sakamoto, A.1    Alia2    Murata, N.3    Murata, A.4
  • 29
    • 0040651623 scopus 로고    scopus 로고
    • Freezing of isolated thylakoid membranes in complex media. X. Interactions among various low molecular weight cryoprotectants
    • Santarius KA (1996) Freezing of isolated thylakoid membranes in complex media. X. Interactions among various low molecular weight cryoprotectants. Cryobiology 33: 118-126
    • (1996) Cryobiology , vol.33 , pp. 118-126
    • Santarius, K.A.1
  • 30
    • 0036072544 scopus 로고    scopus 로고
    • Down-regulation of a chloroplast-targeted beta-amylase leads to starch-excess phenotype in leaves
    • Scheidig A, Fröhlich A, Schulze S, Lloyd JR, Kossmann J (2002) Down-regulation of a chloroplast-targeted beta-amylase leads to starch-excess phenotype in leaves. Plant J 30: 581-591
    • (2002) Plant J , vol.30 , pp. 581-591
    • Scheidig, A.1    Fröhlich, A.2    Schulze, S.3    Lloyd, J.R.4    Kossmann, J.5
  • 31
    • 0742267790 scopus 로고    scopus 로고
    • Maltose is the major form of carbon exported from the chloroplast at night
    • Sean EW, Weber APM, Sharkey TD (2004) Maltose is the major form of carbon exported from the chloroplast at night. Planta 218: 474-482
    • (2004) Planta , vol.218 , pp. 474-482
    • Sean, E.W.1    Weber, A.P.M.2    Sharkey, T.D.3
  • 32
  • 33
    • 0036679053 scopus 로고    scopus 로고
    • Monitoring the expression profiles of 7000 Arabidopsis genes under drought cold and high-salinity stresses using a full-length cDNA microarray
    • Seki M, Narusaka M, Ishida J, Nanjo T, Fujita M, Oono Y, Kamiya A, Nakajima M, Enju A, Sakurai T, et al (2002) Monitoring the expression profiles of 7000 Arabidopsis genes under drought cold and high-salinity stresses using a full-length cDNA microarray. Plant J 31: 279-292
    • (2002) Plant J , vol.31 , pp. 279-292
    • Seki, M.1    Narusaka, M.2    Ishida, J.3    Nanjo, T.4    Fujita, M.5    Oono, Y.6    Kamiya, A.7    Nakajima, M.8    Enju, A.9    Sakurai, T.10
  • 34
    • 0006088395 scopus 로고
    • Sequential control of phytochome-mediated synthesis de novo of beta-amylase in cotyledons of mustard (Sinapis alba L.) seedlings
    • Sharma R, Schopfer P (1982) Sequential control of phytochome-mediated synthesis de novo of beta-amylase in cotyledons of mustard (Sinapis alba L.) seedlings. Planta 155: 183-189
    • (1982) Planta , vol.155 , pp. 183-189
    • Sharma, R.1    Schopfer, P.2
  • 35
    • 84897584785 scopus 로고
    • Release and activity of bound beta-amylase in germinating barley grain
    • Sopanen T, Lauriere C (1989) Release and activity of bound beta-amylase in germinating barley grain. Plant Physiol 89: 244-249
    • (1989) Plant Physiol , vol.89 , pp. 244-249
    • Sopanen, T.1    Lauriere, C.2
  • 36
    • 0028843003 scopus 로고
    • The role of pea chloroplast (alpha) glucosidase in transitory starch degradation
    • Sun Z, Duke SH, Henson CA (1995) The role of pea chloroplast (alpha) glucosidase in transitory starch degradation. Plant Physiol 108: 211-217
    • (1995) Plant Physiol , vol.108 , pp. 211-217
    • Sun, Z.1    Duke, S.H.2    Henson, C.A.3
  • 38
    • 0035979317 scopus 로고    scopus 로고
    • Multiple transcription-factor genes are early targets of phytochome A signaling
    • Tepperman JM, Zhu T, Chang HS, Wang X, Quail PH (2001) Multiple transcription-factor genes are early targets of phytochome A signaling. Proc Natl Acad Sci USA 98: 9437-9442
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9437-9442
    • Tepperman, J.M.1    Zhu, T.2    Chang, H.S.3    Wang, X.4    Quail, P.H.5
  • 39
    • 0029845178 scopus 로고    scopus 로고
    • Phytohormone-regulated beta-amylase gene expression in rice
    • Wang S-M, Lue W-L, Eimert K, Chen J (1996) Phytohormone-regulated beta-amylase gene expression in rice. Plant Mol Biol 31: 975-982
    • (1996) Plant Mol Biol , vol.31 , pp. 975-982
    • Wang, S.-M.1    Lue, W.-L.2    Eimert, K.3    Chen, J.4
  • 41
    • 0009282853 scopus 로고
    • Carbohydrate accumulation in leaves and stems of "Valencia" orange at progressively colder temperatures
    • Yelenosky G, Guy CL (1977) Carbohydrate accumulation in leaves and stems of "Valencia" orange at progressively colder temperatures. Bot Gaz 138: 13-17
    • (1977) Bot Gaz , vol.138 , pp. 13-17
    • Yelenosky, G.1    Guy, C.L.2
  • 42
    • 0001614498 scopus 로고
    • Exoamylase activity in vacuoles isolated from pea and wheat leaf protoplast
    • Ziegler P, Beck E (1986) Exoamylase activity in vacuoles isolated from pea and wheat leaf protoplast. Plant Physiol 82: 1119-1121
    • (1986) Plant Physiol , vol.82 , pp. 1119-1121
    • Ziegler, P.1    Beck, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.