메뉴 건너뛰기




Volumn 28, Issue 4, 2010, Pages 620-626

Cloning and characterization of a maize cDNA encoding glutamate decarboxylase

Author keywords

Activity; Expression; Glutamate decarboxylase; Stress; Zea mays

Indexed keywords

ESCHERICHIA COLI; ZEA MAYS;

EID: 77954427218     PISSN: 07359640     EISSN: 15729818     Source Type: Journal    
DOI: 10.1007/s11105-010-0191-3     Document Type: Article
Times cited : (21)

References (21)
  • 1
    • 0035977492 scopus 로고    scopus 로고
    • Rice (Oryza sativa) contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus
    • doi:10.1016/S0167-4781(01)00324-4
    • Akama K, Akihiro T, Kitagawa M et al (2001) Rice (Oryza sativa) contains a novel isoform of glutamate decarboxylase that lacks an authentic calmodulin-binding domain at the C-terminus. Biochim Biophys Acta 1522: 143-150. doi: 10. 1016/S0167-4781(01)00324-4.
    • (2001) Biochim Biophys Acta , vol.1522 , pp. 143-150
    • Akama, K.1    Akihiro, T.2    Kitagawa, M.3
  • 2
    • 0029310677 scopus 로고
    • Molecular and biochemical analysis of calmodulin interactions with the calmodulin-binding domain of plant glutamate decarboxylase
    • Arazi T, Baum G, Snedden WA et al (1995) Molecular and biochemical analysis of calmodulin interactions with the calmodulin-binding domain of plant glutamate decarboxylase. Plant Physiol 108: 551-561.
    • (1995) Plant Physiol , vol.108 , pp. 551-561
    • Arazi, T.1    Baum, G.2    Snedden, W.A.3
  • 3
    • 0027203970 scopus 로고
    • A plant glutamate decarboxylase containing a calmodulin binding domain. Cloning, sequence, and functional analysis
    • Baum G, Chen Y, Arazi T et al (1993) A plant glutamate decarboxylase containing a calmodulin binding domain. Cloning, sequence, and functional analysis. J Biol Chem 268: 19610-19617.
    • (1993) J Biol Chem , vol.268 , pp. 19610-19617
    • Baum, G.1    Chen, Y.2    Arazi, T.3
  • 4
    • 1542290398 scopus 로고    scopus 로고
    • GABA in plants: Just a metabolite?
    • doi:10.1016/j.tplants.2004.01.006
    • Bouché N, Fromm H (2004) GABA in plants: just a metabolite? Trends Plant Sci 9: 110-116. doi: 10. 1016/j. tplants. 2004. 01. 006.
    • (2004) Trends Plant Sci , vol.9 , pp. 110-116
    • Bouché, N.1    Fromm, H.2
  • 5
    • 16544368713 scopus 로고    scopus 로고
    • The root-specific glutamate decarboxylase (GAD1) is essential for sustaining GABA levels in Arabidopsis
    • doi:10.1007/s11103-004-0650-z
    • Bouché N, Fait A, Zik M et al (2004) The root-specific glutamate decarboxylase (GAD1) is essential for sustaining GABA levels in Arabidopsis. Plant Mol Biol 55: 315-325. doi: 10. 1007/s11103-004-0650-z.
    • (2004) Plant Mol Biol , vol.55 , pp. 315-325
    • Bouché, N.1    Fait, A.2    Zik, M.3
  • 6
    • 0028191604 scopus 로고
    • The 58-kilodahon calmodulin binding glutamate decarboxylase is a ubiquitous protein in petunia organs and its expression is developmentally regulated
    • Chen Y, Baum G, Fromm H (1994) The 58-kilodahon calmodulin binding glutamate decarboxylase is a ubiquitous protein in petunia organs and its expression is developmentally regulated. Plant Physiol 106: 1381-1387.
    • (1994) Plant Physiol , vol.106 , pp. 1381-1387
    • Chen, Y.1    Baum, G.2    Fromm, H.3
  • 7
    • 0029257403 scopus 로고
    • A role for glutamate decarboxylase during tomato ripening: The characterisation of a cDNA encoding a putative glutamate decarboxylase with a calmodulin-binding site
    • doi:10.1007/BF00020887
    • Gallego PP, Whotton L, Picton S et al (1995) A role for glutamate decarboxylase during tomato ripening: the characterisation of a cDNA encoding a putative glutamate decarboxylase with a calmodulin-binding site. Plant Mol Biol 27: 1143-1151. doi: 10. 1007/BF00020887.
    • (1995) Plant Mol Biol , vol.27 , pp. 1143-1151
    • Gallego, P.P.1    Whotton, L.2    Picton, S.3
  • 8
    • 0030879974 scopus 로고    scopus 로고
    • Purification and characterization of glutamate decarboxylase from cowpea
    • doi::10.1016/S0031-9422(97)00236-7
    • Johanson BS, Singh NK, Cherry JH et al (1997) Purification and characterization of glutamate decarboxylase from cowpea. Phytochemical 46: 39-44. doi:: 10. 1016/S0031-9422(97)00236-7.
    • (1997) Phytochemical , vol.46 , pp. 39-44
    • Johanson, B.S.1    Singh, N.K.2    Cherry, J.H.3
  • 9
    • 0035638731 scopus 로고    scopus 로고
    • Inactivation of brain glutamate dehydrogenase isoproteins by MDL 29951
    • Lee EY, Yoon HY, Kim TU et al (2001) Inactivation of brain glutamate dehydrogenase isoproteins by MDL 29951. J Biochem Mol Biol 34: 268-273.
    • (2001) J Biochem Mol Biol , vol.34 , pp. 268-273
    • Lee, E.Y.1    Yoon, H.Y.2    Kim, T.U.3
  • 10
    • 0036085047 scopus 로고    scopus 로고
    • PlantCARE, a database of plant cis-acting regulatory elements and a portal to tools for in silico analysis of promoter sequences
    • Lescot M, Déhais P, Thijs G et al (2002) PlantCARE, a database of plant cis-acting regulatory elements and a portal to tools for in silico analysis of promoter sequences. Nucleic Acids Res 30: 325-327.
    • (2002) Nucleic Acids Res , vol.30 , pp. 325-327
    • Lescot, M.1    Déhais, P.2    Thijs, G.3
  • 11
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • doi:10.1006/meth.2001.1262
    • Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25: 402-408. doi: 10. 1006/meth. 2001. 1262.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 12
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissues
    • doi:10.1111/j.1399-3054.1962.tb08052.x
    • Murashige T, Skoog F (1962) A revised medium for rapid growth and bioassays with tobacco tissues. Plant Physiol 15: 473-497. doi: 10. 1111/j. 1399-3054. 1962. tb08052. x.
    • (1962) Plant Physiol , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 13
    • 27144501466 scopus 로고    scopus 로고
    • Cloning and characterization of a rice cDNA encoding glutamate decarboxylase
    • Ohs H, Choi WG, Lee IT et al (2005) Cloning and characterization of a rice cDNA encoding glutamate decarboxylase. J Biochem Mol Biol 38: 595-601.
    • (2005) J Biochem Mol Biol , vol.38 , pp. 595-601
    • Ohs, H.1    Choi, W.G.2    Lee, I.T.3
  • 14
    • 0032731314 scopus 로고    scopus 로고
    • Metabolism and functions of gamma-aminobutyric acid
    • doi:10.1016/S1360-1385(99)01486-7
    • Shelp BJ, Bown AW, McLean MD (1999) Metabolism and functions of gamma-aminobutyric acid. Trends Plant Sci 4: 446-452. doi: 10. 1016/S1360-1385(99)01486-7.
    • (1999) Trends Plant Sci , vol.4 , pp. 446-452
    • Shelp, B.J.1    Bown, A.W.2    McLean, M.D.3
  • 15
    • 0028830815 scopus 로고
    • Calcium/calmodulin activation of soybean glutamate decarboxylase
    • Snedden WA, Arazi T, Fromm H et al (1995) Calcium/calmodulin activation of soybean glutamate decarboxylase. Plant Physiol 108: 543-549.
    • (1995) Plant Physiol , vol.108 , pp. 543-549
    • Snedden, W.A.1    Arazi, T.2    Fromm, H.3
  • 16
    • 0030060208 scopus 로고    scopus 로고
    • Activation of a recombinant petunia glutamate decarboxylase by calcium/calmodulin or by a monoclonal antibody which recognizes the calmodulin binding domain
    • Snedden WA, Koutsia N, Baum G et al (1996) Activation of a recombinant petunia glutamate decarboxylase by calcium/calmodulin or by a monoclonal antibody which recognizes the calmodulin binding domain. J Biol Chem 271: 4148-4153.
    • (1996) J Biol Chem , vol.271 , pp. 4148-4153
    • Snedden, W.A.1    Koutsia, N.2    Baum, G.3
  • 17
    • 0032135219 scopus 로고    scopus 로고
    • Characterization of two glutamate decarboxylase cDNA clones from Arabidopsis
    • Turano FJ, Fang TK (1998) Characterization of two glutamate decarboxylase cDNA clones from Arabidopsis. Plant Physiol 117: 1411-1421.
    • (1998) Plant Physiol , vol.117 , pp. 1411-1421
    • Turano, F.J.1    Fang, T.K.2
  • 18
    • 0000955919 scopus 로고
    • Rapid accumulation of gamma-aminobutyric acid and alanine in soybean leaves in response to an abrupt transfer to lower temperature, darkness, or mechanical manipulation
    • Wallace W, Secor J, Schrader LE (1984) Rapid accumulation of gamma-aminobutyric acid and alanine in soybean leaves in response to an abrupt transfer to lower temperature, darkness, or mechanical manipulation. Plant Physiol 75: 170-175.
    • (1984) Plant Physiol , vol.75 , pp. 170-175
    • Wallace, W.1    Secor, J.2    Schrader, L.E.3
  • 19
    • 0032580023 scopus 로고    scopus 로고
    • Cloning and characterization of a tobacco cDNA encoding calcium/calmodulin-dependent glutamate decarboxylase
    • Yuns J, Ohs H (1998) Cloning and characterization of a tobacco cDNA encoding calcium/calmodulin-dependent glutamate decarboxylase. Mol Cells 8: 125-129.
    • (1998) Mol Cells , vol.8 , pp. 125-129
    • Yuns, J.1    Ohs, H.2
  • 20
    • 36448980672 scopus 로고    scopus 로고
    • Effects of water-deficit stress on the transcriptomes of developing immature ear and tassel in maize
    • doi:10.1007/s00299-007-0419-3
    • Zhuang Y, Ren G, Yue G et al (2007) Effects of water-deficit stress on the transcriptomes of developing immature ear and tassel in maize. Plant Cell Rep 26: 2137-2147. doi: 10. 1007/s00299-007-0419-3.
    • (2007) Plant Cell Rep , vol.26 , pp. 2137-2147
    • Zhuang, Y.1    Ren, G.2    Yue, G.3
  • 21
    • 0032146950 scopus 로고    scopus 로고
    • Two isoforms of glutamate decarboxylase in Arabidopsis are regulated by calcium/calmodulin and differ in organ distribution
    • doi:10.1023/A:1006047623263
    • Zik M, Arazi T, Snedden WA et al (1998) Two isoforms of glutamate decarboxylase in Arabidopsis are regulated by calcium/calmodulin and differ in organ distribution. Plant Mol Biol 37: 967-975. doi: 10. 1023/A: 1006047623263.
    • (1998) Plant Mol Biol , vol.37 , pp. 967-975
    • Zik, M.1    Arazi, T.2    Snedden, W.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.