메뉴 건너뛰기




Volumn 46, Issue 4, 2008, Pages 444-451

Differential regulation of phenylalanine ammonia lyase activity and protein level by light in tomato seedlings

Author keywords

Phenylalanine ammonia lyase; Phosphorylation; Phytochrome; Protein inactivation; Tomato

Indexed keywords

ISOENZYME; PHENYLALANINE AMMONIA LYASE;

EID: 42049097247     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2008.02.001     Document Type: Article
Times cited : (34)

References (41)
  • 1
    • 0035983890 scopus 로고    scopus 로고
    • Regulation of CDPKs, including identification of PAL kinase, in biotically stressed cells of French bean
    • Allwood E.G., Davies D.R., Gerrish C., and Bolwell G.P. Regulation of CDPKs, including identification of PAL kinase, in biotically stressed cells of French bean. Plant. Mol. Biol. 49 (2002) 533-544
    • (2002) Plant. Mol. Biol. , vol.49 , pp. 533-544
    • Allwood, E.G.1    Davies, D.R.2    Gerrish, C.3    Bolwell, G.P.4
  • 2
    • 0032811334 scopus 로고    scopus 로고
    • Phosphorylation of phenylalanine ammonia-lyase, evidence for a novel protein kinase and identification of the phosphorylated residue
    • Allwood E.G., Davies D.R., Gerrish C., Ellis B.E., and Bolwell G.P. Phosphorylation of phenylalanine ammonia-lyase, evidence for a novel protein kinase and identification of the phosphorylated residue. FEBS Lett. 457 (1999) 47-52
    • (1999) FEBS Lett. , vol.457 , pp. 47-52
    • Allwood, E.G.1    Davies, D.R.2    Gerrish, C.3    Ellis, B.E.4    Bolwell, G.P.5
  • 3
    • 0033759391 scopus 로고    scopus 로고
    • Altering expression of cinnamic acid 4-hydroxylase in transgenic plants provides evidence for a feedback loop at the entry point into the phenylpropanoid pathway
    • Blount J.W., Korth K.L., Masoud S.A., Rasmussen S., Lamb C., and Dixon R.A. Altering expression of cinnamic acid 4-hydroxylase in transgenic plants provides evidence for a feedback loop at the entry point into the phenylpropanoid pathway. Plant Physiol. 122 (2000) 107-116
    • (2000) Plant Physiol. , vol.122 , pp. 107-116
    • Blount, J.W.1    Korth, K.L.2    Masoud, S.A.3    Rasmussen, S.4    Lamb, C.5    Dixon, R.A.6
  • 4
    • 0002535074 scopus 로고
    • l- Phenylalanine ammonia-lyase from Phaseolus vulgaris: modulation of the levels of active enzyme by trans-cinnamic acid
    • Bolwell G.P., Cramer C.L., Lamb C.J., Schuch W., and Dixon R.A. l- Phenylalanine ammonia-lyase from Phaseolus vulgaris: modulation of the levels of active enzyme by trans-cinnamic acid. Planta 169 (1986) 97-107
    • (1986) Planta , vol.169 , pp. 97-107
    • Bolwell, G.P.1    Cramer, C.L.2    Lamb, C.J.3    Schuch, W.4    Dixon, R.A.5
  • 5
    • 0001240165 scopus 로고
    • A role for phosphorylation in the down-regulation of phenylalanine ammonia-lyase in suspension-cultured cells of French bean
    • Bolwell G.P. A role for phosphorylation in the down-regulation of phenylalanine ammonia-lyase in suspension-cultured cells of French bean. Phytochemistry 31 (1992) 4081-4086
    • (1992) Phytochemistry , vol.31 , pp. 4081-4086
    • Bolwell, G.P.1
  • 6
    • 0004889886 scopus 로고
    • Use of immunotitration to demonstrate phytochrome-mediated de novo synthesis of chalcone synthase and phenylalanine ammonia-lyase in mustard seedling cotyledons, Z
    • Brodenfeldt R., and Mohr H. Use of immunotitration to demonstrate phytochrome-mediated de novo synthesis of chalcone synthase and phenylalanine ammonia-lyase in mustard seedling cotyledons, Z. Naturforsch 41 (1986) 61-68
    • (1986) Naturforsch , vol.41 , pp. 61-68
    • Brodenfeldt, R.1    Mohr, H.2
  • 7
    • 0035902967 scopus 로고    scopus 로고
    • Molecular identification of phenylalanine ammonia-lyase as a substrate of a specific constitutively active Arabidopsis CDPK expressed in maize protoplasts
    • Cheng S.-H., Sheen J., Gerrish C., and Burwells G.P. Molecular identification of phenylalanine ammonia-lyase as a substrate of a specific constitutively active Arabidopsis CDPK expressed in maize protoplasts. FEBS Lett. 503 (2001) 185-188
    • (2001) FEBS Lett. , vol.503 , pp. 185-188
    • Cheng, S.-H.1    Sheen, J.2    Gerrish, C.3    Burwells, G.P.4
  • 8
    • 0036598460 scopus 로고    scopus 로고
    • Transcriptional profiling reveals novel interactions between wounding, pathogen, abiotic stress, and hormonal responses in Arabidopsis
    • Cheong Y., Chang H., Gupta R., Wang X., Zhu T., and Luan S. Transcriptional profiling reveals novel interactions between wounding, pathogen, abiotic stress, and hormonal responses in Arabidopsis. Plant Physiol. 129 (2002) 661-677
    • (2002) Plant Physiol. , vol.129 , pp. 661-677
    • Cheong, Y.1    Chang, H.2    Gupta, R.3    Wang, X.4    Zhu, T.5    Luan, S.6
  • 9
    • 0343125631 scopus 로고
    • The role of enzyme inactivation in the regulation of synthetic pathways: a case history
    • Creasy L.L. The role of enzyme inactivation in the regulation of synthetic pathways: a case history. Physiol. Plant. 71 (1987) 389-392
    • (1987) Physiol. Plant. , vol.71 , pp. 389-392
    • Creasy, L.L.1
  • 10
    • 0001031206 scopus 로고
    • Photoregulation of phenylalanine ammonia lyase is not correlated with anthocyanin induction in photomorphogenic mutants of tomato (Lycopersicon esculentum)
    • Goud K.V., Sharma R., Kendrick R.E., and Furuya M. Photoregulation of phenylalanine ammonia lyase is not correlated with anthocyanin induction in photomorphogenic mutants of tomato (Lycopersicon esculentum). Plant Cell Physiol. 32 (1991) 1251-1258
    • (1991) Plant Cell Physiol. , vol.32 , pp. 1251-1258
    • Goud, K.V.1    Sharma, R.2    Kendrick, R.E.3    Furuya, M.4
  • 11
    • 0000089537 scopus 로고
    • Enzymic controls in the biosynthesis of lignins and flavonoids
    • Hahlbrock K., and Grisebach H. Enzymic controls in the biosynthesis of lignins and flavonoids. Annu. Rev. Plant Physiol. 30 (1979) 105-130
    • (1979) Annu. Rev. Plant Physiol. , vol.30 , pp. 105-130
    • Hahlbrock, K.1    Grisebach, H.2
  • 13
    • 0030468571 scopus 로고    scopus 로고
    • Overexpression of l-phenylalanine ammonia-lyase in transgenic tobacco plants reveals control points for flux into phenylpropanoid biosynthesis
    • Howles P.A., Sewalt V.J.H., Paiva N.L., Elkind Y., Bate N.J., Lamb C., and Dixon R.A. Overexpression of l-phenylalanine ammonia-lyase in transgenic tobacco plants reveals control points for flux into phenylpropanoid biosynthesis. Plant Physiol. 112 (1996) 1617-1624
    • (1996) Plant Physiol. , vol.112 , pp. 1617-1624
    • Howles, P.A.1    Sewalt, V.J.H.2    Paiva, N.L.3    Elkind, Y.4    Bate, N.J.5    Lamb, C.6    Dixon, R.A.7
  • 14
    • 0035983678 scopus 로고    scopus 로고
    • The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis
    • Kerk D., Bulgrien J., Smith D.W., Barsam B., Veretnik S., and Gribskov M. The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis. Plant Physiol. 129 (2002) 908-925
    • (2002) Plant Physiol. , vol.129 , pp. 908-925
    • Kerk, D.1    Bulgrien, J.2    Smith, D.W.3    Barsam, B.4    Veretnik, S.5    Gribskov, M.6
  • 16
    • 0034805320 scopus 로고    scopus 로고
    • The phenylalanine ammonia-lyase gene family in raspberry. Structure, expression, and evolution
    • Kumar A., and Ellis B.E. The phenylalanine ammonia-lyase gene family in raspberry. Structure, expression, and evolution. Plant Physiol. 127 (2001) 230-239
    • (2001) Plant Physiol. , vol.127 , pp. 230-239
    • Kumar, A.1    Ellis, B.E.2
  • 17
    • 0019390337 scopus 로고
    • Density labelling characterisation of the effects of cordycepin and cycloheximide on the turnover of phenylalanine ammonia-lyase
    • Lamb C.J., Lawton M.A., and Shields S.E. Density labelling characterisation of the effects of cordycepin and cycloheximide on the turnover of phenylalanine ammonia-lyase. Biochim. Biophys. Acta 675 (1981) 1-8
    • (1981) Biochim. Biophys. Acta , vol.675 , pp. 1-8
    • Lamb, C.J.1    Lawton, M.A.2    Shields, S.E.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0026637937 scopus 로고
    • Truncated phenylalanine ammonia-lyase expression in tomato (Lycopersicon esculentum)
    • Lee S.W., Robb J.E., and Nazar R.N. Truncated phenylalanine ammonia-lyase expression in tomato (Lycopersicon esculentum). J. Biol. Chem. 267 (1992) 11824-11830
    • (1992) J. Biol. Chem. , vol.267 , pp. 11824-11830
    • Lee, S.W.1    Robb, J.E.2    Nazar, R.N.3
  • 20
    • 0024978438 scopus 로고
    • Differential regulation of phenylalanine ammonia-lyase genes during plant development and by environmental cues
    • Liang X.W., Dron M., Cramer C.L., Dixon R.A., and Lamb C.J. Differential regulation of phenylalanine ammonia-lyase genes during plant development and by environmental cues. J. Biol. Chem. 264 (1989) 14486-14492
    • (1989) J. Biol. Chem. , vol.264 , pp. 14486-14492
    • Liang, X.W.1    Dron, M.2    Cramer, C.L.3    Dixon, R.A.4    Lamb, C.J.5
  • 22
    • 0142057022 scopus 로고    scopus 로고
    • Protein phosphatases in plants
    • Luan S. Protein phosphatases in plants. Annu. Rev. Plant Biol. 54 (2003) 63-92
    • (2003) Annu. Rev. Plant Biol. , vol.54 , pp. 63-92
    • Luan, S.1
  • 23
    • 0035115228 scopus 로고    scopus 로고
    • The ABI1 and ABI2 protein phosphatases 2C act in a negative feedback regulatory loop of the abscisic acid signalling pathway
    • Merlot S., Gosti F., Guerrier D., Vavasseur A., and Giraudat J. The ABI1 and ABI2 protein phosphatases 2C act in a negative feedback regulatory loop of the abscisic acid signalling pathway. Plant J. 25 (2001) 295-303
    • (2001) Plant J. , vol.25 , pp. 295-303
    • Merlot, S.1    Gosti, F.2    Guerrier, D.3    Vavasseur, A.4    Giraudat, J.5
  • 24
    • 0030250857 scopus 로고    scopus 로고
    • Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin
    • Moorhead G., Douglas P., Morrice N., Scarabel M., Aitken A., and MacKintosh C. Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccin. Curr. Biol. 6 (1996) 1104-1113
    • (1996) Curr. Biol. , vol.6 , pp. 1104-1113
    • Moorhead, G.1    Douglas, P.2    Morrice, N.3    Scarabel, M.4    Aitken, A.5    MacKintosh, C.6
  • 25
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige T., and Skoog F. A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol. Plant. 15 (1962) 473-497
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 26
    • 0032725627 scopus 로고    scopus 로고
    • Transgene-mediated and elicitor-induced perturbation of metabolic channeling at the entry point into the phenylpropanoid pathway
    • Rasmussen S., and Dixon R.A. Transgene-mediated and elicitor-induced perturbation of metabolic channeling at the entry point into the phenylpropanoid pathway. Plant Cell 11 (1999) 1537-1551
    • (1999) Plant Cell , vol.11 , pp. 1537-1551
    • Rasmussen, S.1    Dixon, R.A.2
  • 27
    • 0028045558 scopus 로고
    • UV-B responsive anthocyanin production in a rice cultivar is associated with a specific phase of phenylalanine ammonia lyase biosynthesis
    • Reddy V.S., Goud K.V., Sharma R., and Reddy A.R. UV-B responsive anthocyanin production in a rice cultivar is associated with a specific phase of phenylalanine ammonia lyase biosynthesis. Plant Physiol. 105 (1994) 1059-1066
    • (1994) Plant Physiol. , vol.105 , pp. 1059-1066
    • Reddy, V.S.1    Goud, K.V.2    Sharma, R.3    Reddy, A.R.4
  • 28
    • 0023473794 scopus 로고
    • Rapid isoelectric focussing in a vertical polyacrylamide minigel system
    • Robertson E.F., Dannelly H.K., Malloy P.J., and Reeves H.C. Rapid isoelectric focussing in a vertical polyacrylamide minigel system. Anal. Biochem. 167 (1987) 290-294
    • (1987) Anal. Biochem. , vol.167 , pp. 290-294
    • Robertson, E.F.1    Dannelly, H.K.2    Malloy, P.J.3    Reeves, H.C.4
  • 29
    • 0032513155 scopus 로고    scopus 로고
    • Regulation of a plant plasma membrane sucrose transporter by phosphorylation
    • Roblin G., Sakr S., Bonmort J., and Delrot S. Regulation of a plant plasma membrane sucrose transporter by phosphorylation. FEBS Lett. 424 (1998) 165-168
    • (1998) FEBS Lett. , vol.424 , pp. 165-168
    • Roblin, G.1    Sakr, S.2    Bonmort, J.3    Delrot, S.4
  • 30
    • 0032973377 scopus 로고    scopus 로고
    • Purification and characterization of UV-B induced phenylalanine ammonia lyase from rice seedlings
    • Sarma A.D., and Sharma R. Purification and characterization of UV-B induced phenylalanine ammonia lyase from rice seedlings. Phytochemistry 50 (1999) 729-737
    • (1999) Phytochemistry , vol.50 , pp. 729-737
    • Sarma, A.D.1    Sharma, R.2
  • 31
    • 0032414009 scopus 로고    scopus 로고
    • Differential expression and properties of phenylalanine ammonia-lyase isoforms in tomato leaves
    • Sarma A.D., Sreelakshmi Y., and Sharma R. Differential expression and properties of phenylalanine ammonia-lyase isoforms in tomato leaves. Phytochemistry 49 (1998) 2233-2243
    • (1998) Phytochemistry , vol.49 , pp. 2233-2243
    • Sarma, A.D.1    Sreelakshmi, Y.2    Sharma, R.3
  • 32
    • 0041113470 scopus 로고
    • Phytochrome controlled phenylalanine ammonia lyase activity in Hordeum vulgare plastids
    • Saunders J.A., and McClure J.W. Phytochrome controlled phenylalanine ammonia lyase activity in Hordeum vulgare plastids. Phytochemistry 14 (1975) 1285-1289
    • (1975) Phytochemistry , vol.14 , pp. 1285-1289
    • Saunders, J.A.1    McClure, J.W.2
  • 33
    • 0025349785 scopus 로고
    • Wound-induced phenylalanine ammonia-lyase in potato (Solanum tuberosum) tuber discs. Significance of glycosylation and immunolocalization of enzyme subunits
    • Shaw N.M., Bolwell G.P., and Smith C. Wound-induced phenylalanine ammonia-lyase in potato (Solanum tuberosum) tuber discs. Significance of glycosylation and immunolocalization of enzyme subunits. Biochem. J. 267 (1990) 163-170
    • (1990) Biochem. J. , vol.267 , pp. 163-170
    • Shaw, N.M.1    Bolwell, G.P.2    Smith, C.3
  • 34
    • 0027618491 scopus 로고
    • Transcription of two members of a gene family encoding phenylalanine ammonia-lyase leads to remarkably different cell specificities and induction patterns
    • Shufflebottom D., Edwards K., Schuch W., and Bevan M. Transcription of two members of a gene family encoding phenylalanine ammonia-lyase leads to remarkably different cell specificities and induction patterns. Plant J. 3 (1993) 835-845
    • (1993) Plant J. , vol.3 , pp. 835-845
    • Shufflebottom, D.1    Edwards, K.2    Schuch, W.3    Bevan, M.4
  • 35
    • 0032826224 scopus 로고    scopus 로고
    • Sunlight-induced anthocyanin pigmentation in maize vegetative tissues
    • Singh A., Selvi M.T., and Sharma R. Sunlight-induced anthocyanin pigmentation in maize vegetative tissues. J. Exp. Bot. 50 (1999) 1619-1625
    • (1999) J. Exp. Bot. , vol.50 , pp. 1619-1625
    • Singh, A.1    Selvi, M.T.2    Sharma, R.3
  • 37
    • 42049089341 scopus 로고
    • Absence of Pfr destruction in the modulation of phenylalanine ammonia-lyase synthesis of mustard cotyledons
    • Tong W.F., and Schopfer P. Absence of Pfr destruction in the modulation of phenylalanine ammonia-lyase synthesis of mustard cotyledons. Plant Physiol. 61 (1978) 59-61
    • (1978) Plant Physiol. , vol.61 , pp. 59-61
    • Tong, W.F.1    Schopfer, P.2
  • 38
    • 23044523400 scopus 로고    scopus 로고
    • Carbon and nitrogen metabolism and reversible protein phosphorylation
    • Toroser D., and Huber S.C. Carbon and nitrogen metabolism and reversible protein phosphorylation. Adv. Bot. Res. 32 (2000) 435-458
    • (2000) Adv. Bot. Res. , vol.32 , pp. 435-458
    • Toroser, D.1    Huber, S.C.2
  • 39
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 40
    • 0032082930 scopus 로고    scopus 로고
    • Phenylpropanoid biosynthesis and its regulation
    • Weisshaar B., and Jenkins G.I. Phenylpropanoid biosynthesis and its regulation. Curr. Opin. Plant Biol. 1 (1998) 251-257
    • (1998) Curr. Opin. Plant Biol. , vol.1 , pp. 251-257
    • Weisshaar, B.1    Jenkins, G.I.2
  • 41
    • 0034979805 scopus 로고    scopus 로고
    • Flavonoid biosynthesis: a colorful model for genetics, biochemistry, cell biology and biotechnology
    • Winkel-Shirley B. Flavonoid biosynthesis: a colorful model for genetics, biochemistry, cell biology and biotechnology. Plant Physiol. 126 (2001) 485-493
    • (2001) Plant Physiol. , vol.126 , pp. 485-493
    • Winkel-Shirley, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.