메뉴 건너뛰기




Volumn 289, Issue 12, 2014, Pages 8203-8216

The pseudoenzyme PDX1.2 boosts vitamin B6 biosynthesis under heat and oxidative stress in Arabidopsis

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYST ACTIVITY;

EID: 84896985659     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.540526     Document Type: Article
Times cited : (38)

References (55)
  • 3
    • 0035025630 scopus 로고    scopus 로고
    • Isolation of PDX2, a second novel gene in the pyridoxine biosynthesis pathway of eukaryotes, archaebacteria, and a subset of eubacteria
    • DOI 10.1128/JB.183.11.3383-3390.2001
    • Ehrenshaft, M., and Daub, M. E. (2001) Isolation of PDX2, a second novel gene in the pyridoxine biosynthesis pathway of eukaryotes, archaebacteria, and a subset of eubacteria. J. Bacteriol. 183, 3383-3390 (Pubitemid 32448602)
    • (2001) Journal of Bacteriology , vol.183 , Issue.11 , pp. 3383-3390
    • Ehrenshaft, M.1    Daub, M.E.2
  • 4
    • 0033551830 scopus 로고    scopus 로고
    • The extremely conserved pyroA gene of Aspergillus nidulans is required for pyridoxine synthesis and is required indirectly for resistance to photosensitizers
    • Osmani, A. H., May, G. S., and Osmani, S. A. (1999) The extremely conserved pyroA gene of Aspergillus nidulans is required for pyridoxine synthesis and is required indirectly for resistance to photosensitizers. J. Biol. Chem. 274, 23565-23569
    • (1999) J. Biol. Chem. , vol.274 , pp. 23565-23569
    • Osmani, A.H.1    May, G.S.2    Osmani, S.A.3
  • 6
    • 15744377644 scopus 로고    scopus 로고
    • Reconstitution and biochemical characterization of a new pyridoxal-5′-phosphate biosynthetic pathway
    • DOI 10.1021/ja042792t
    • Burns, K. E., Xiang, Y., Kinsland, C. L., McLafferty, F. W., and Begley, T. P. (2005) Reconstitution and biochemical characterization of a new pyridoxal-5′-phosphate biosynthetic pathway. J. Am. Chem. Soc. 127, 3682-3683 (Pubitemid 40411393)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.11 , pp. 3682-3683
    • Burns, K.E.1    Xiang, Y.2    Kinsland, C.L.3    McLafferty, F.W.4    Begley, T.P.5
  • 7
    • 25444433588 scopus 로고    scopus 로고
    • On the two components of pyridoxal 5′-phosphate synthase from Bacillus subtilis
    • DOI 10.1074/jbc.M501356200
    • Raschle, T., Amrhein, N., and Fitzpatrick, T. B. (2005) On the two components of pyridoxal 5′-phosphate synthase from Bacillus subtilis. J. Biol. Chem. 280, 32291-32300 (Pubitemid 41361838)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.37 , pp. 32291-32300
    • Raschle, T.1    Amrhein, N.2    Fitzpatrick, T.B.3
  • 9
    • 33845468647 scopus 로고    scopus 로고
    • Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima
    • DOI 10.1021/bi061464y
    • Zein, F., Zhang, Y., Kang, Y.-N., Burns, K., Begley, T. P., and Ealick, S. E. (2006) Structural insights into the mechanism of the PLP synthase holoenzyme from Thermotoga maritima. Biochemistry 45, 14609-14620 (Pubitemid 44906977)
    • (2006) Biochemistry , vol.45 , Issue.49 , pp. 14609-14620
    • Zein, F.1    Zhang, Y.2    Kang, Y.-N.3    Burns, K.4    Begley, T.P.5    Ealick, S.E.6
  • 10
    • 1142298586 scopus 로고    scopus 로고
    • Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5′-phosphate biosynthesis
    • Belitsky, B. R. (2004) Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5′-phosphate biosynthesis. J. Bacteriol. 186, 1191-1196
    • (2004) J. Bacteriol. , vol.186 , pp. 1191-1196
    • Belitsky, B.R.1
  • 11
    • 34250658904 scopus 로고    scopus 로고
    • Functional analysis of PDX2 from arabidopsis, a glutaminase involved in vitamin B6 biosynthesis
    • DOI 10.1104/pp.107.096784
    • Tambasco-Studart, M., Tews, I., Amrhein, N., and Fitzpatrick, T. B. (2007) Functional analysis of PDX2 from Arabidopsis thaliana, a glutaminase involved in vitamin B6 biosynthesis. Plant Physiol. 144, 915-925 (Pubitemid 46944754)
    • (2007) Plant Physiology , vol.144 , Issue.2 , pp. 915-925
    • Tambasco-Studart, M.1    Tews, I.2    Amrhein, N.3    Fitzpatrick, T.B.4
  • 12
    • 33644834147 scopus 로고    scopus 로고
    • Pyridoxine is required for post-embryonic root development and tolerance to osmotic and oxidative stresses
    • Chen, H., and Xiong, L. (2005) Pyridoxine is required for post-embryonic root development and tolerance to osmotic and oxidative stresses. Plant J. 44, 396-408
    • (2005) Plant J. , vol.44 , pp. 396-408
    • Chen, H.1    Xiong, L.2
  • 13
    • 33947280872 scopus 로고    scopus 로고
    • 6 biosynthesis genes by abiotic stress
    • DOI 10.1016/j.plaphy.2007.01.007, PII S0981942807000101
    • Denslow, S. A., Rueschhoff, E. E., and Daub, M. E. (2007) Regulation of the Arabidopsis thaliana vitamin B6 biosynthesis genes by abiotic stress. Plant Physiol. Biochem. 45, 152-161 (Pubitemid 46436510)
    • (2007) Plant Physiology and Biochemistry , vol.45 , Issue.2 , pp. 152-161
    • Denslow, S.A.1    Rueschhoff, E.E.2    Daub, M.E.3
  • 14
    • 28944438321 scopus 로고    scopus 로고
    • 6 vitamers during plant defense responses
    • DOI 10.1016/j.pmpp.2005.09.004, PII S0885576505001633
    • Denslow, S. A., Walls, A. A., and Daub, M. E. (2005) Regulation of biosynthetic genes and antioxidant properties of vitamin B6 vitamers during plant defense responses. Physiol. Mol. Plant Pathol. 66, 244-255 (Pubitemid 41785480)
    • (2005) Physiological and Molecular Plant Pathology , vol.66 , Issue.6 , pp. 244-255
    • Denslow, S.A.1    Walls, A.A.2    Daub, M.E.3
  • 15
    • 84859464651 scopus 로고    scopus 로고
    • The antioxidative effect of de novo generated vitamin B6 in Plasmodium falciparum validated by protein interference
    • Knöckel, J., Müller, I. B., Butzloff, S., Bergmann, B., Walter, R. D., and Wrenger, C. (2012) The antioxidative effect of de novo generated vitamin B6 in Plasmodium falciparum validated by protein interference. Biochem. J. 443, 397-405
    • (2012) Biochem. J. , vol.443 , pp. 397-405
    • Knöckel, J.1    Müller, I.B.2    Butzloff, S.3    Bergmann, B.4    Walter, R.D.5    Wrenger, C.6
  • 17
    • 33845521845 scopus 로고    scopus 로고
    • PDX1 is essential for vitamin B6 biosynthesis, development and stress tolerance in Arabidopsis
    • DOI 10.1111/j.1365-313X.2006.02928.x
    • Titiz, O., Tambasco-Studart, M., Warzych, E., Apel, K., Amrhein, N., Laloi, C., and Fitzpatrick, T. B. (2006) PDX1 is essential for vitamin B6 biosynthesis, development and stress tolerance in Arabidopsis. Plant J. 48, 933-946 (Pubitemid 44924353)
    • (2006) Plant Journal , vol.48 , Issue.6 , pp. 933-946
    • Titiz, O.1    Tambasco-Studart, M.2    Warzych, E.3    Apel, K.4    Amrhein, N.5    Laloi, C.6    Fitzpatrick, T.B.7
  • 18
    • 0034132391 scopus 로고    scopus 로고
    • Vitamin B6 (Pyridoxine) and its derivatives are efficient singlet oxygen quenchers and potential fungal antioxidants
    • Bilski, P., Li, M. Y., Ehrenshaft, M., Daub, M. E., and Chignell, C. F. (2000) Vitamin B6 (Pyridoxine) and its derivatives are efficient singlet oxygen quenchers and potential fungal antioxidants. Photochem. Photobiol. 71, 129-134
    • (2000) Photochem. Photobiol. , vol.71 , pp. 129-134
    • Bilski, P.1    Li, M.Y.2    Ehrenshaft, M.3    Daub, M.E.4    Chignell, C.F.5
  • 21
    • 38949210195 scopus 로고    scopus 로고
    • The Pdx1 family is structurally and functionally conserved between Arabidopsis thaliana and Ginkgo biloba
    • DOI 10.1111/j.1742-4658.2008.06275.x
    • Leuendorf, J. E., Genau, A., Szewczyk, A., Mooney, S., Drewke, C., Leistner, E., and Hellmann, H. (2008) The Pdx1 family is structurally and functionally conserved between Arabidopsis thaliana and Ginkgo biloba. FEBS J. 275, 960-969 (Pubitemid 351230218)
    • (2008) FEBS Journal , vol.275 , Issue.5 , pp. 960-969
    • Leuendorf, J.E.1    Genau, A.2    Szewczyk, A.3    Mooney, S.4    Drewke, C.5    Leistner, E.6    Hellmann, H.7
  • 23
    • 2942700177 scopus 로고    scopus 로고
    • Inactive enzyme-homologues find new function in regulatory processes
    • DOI 10.1016/j.jmb.2004.04.063, PII S0022283604005248
    • Pils, B., and Schultz, J. (2004) Inactive enzyme homologues find new function in regulatory processes. J. Mol. Biol. 340, 399-404 (Pubitemid 38797988)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.3 , pp. 399-404
    • Pils, B.1    Schultz, J.2
  • 24
    • 84864279894 scopus 로고    scopus 로고
    • New lives for old. Evolution of pseudoenzyme function illustrated by iRhoms
    • Adrain, C., and Freeman, M. (2012) New lives for old. Evolution of pseudoenzyme function illustrated by iRhoms. Nat. Rev. Mol. Cell Biol. 13, 489-498
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 489-498
    • Adrain, C.1    Freeman, M.2
  • 25
    • 84876339450 scopus 로고    scopus 로고
    • "Dead" enzymes show signs of life
    • Leslie, M. (2013) "Dead" enzymes show signs of life. Science 340, 25-27
    • (2013) Science , vol.340 , pp. 25-27
    • Leslie, M.1
  • 26
    • 77957298297 scopus 로고    scopus 로고
    • Complex assembly and metabolic profiling of Arabidopsis thaliana plants overexpressing vitamin B biosynthesis proteins
    • Leuendorf, J. E., Osorio, S., Szewczyk, A., Fernie, A. R., and Hellmann, H. (2010) Complex assembly and metabolic profiling of Arabidopsis thaliana plants overexpressing vitamin B biosynthesis proteins. Mol. Plant 3, 890-903
    • (2010) Mol. Plant , vol.3 , pp. 890-903
    • Leuendorf, J.E.1    Osorio, S.2    Szewczyk, A.3    Fernie, A.R.4    Hellmann, H.5
  • 27
    • 33745791496 scopus 로고    scopus 로고
    • Analysis of the Arabidopsis rsr4-1/pdx1-3 mutant reveals the critical function of the PDX1 protein family in metabolism, development, and vitamin B6 biosynthesis
    • DOI 10.1105/tpc.105.036269
    • Wagner, S., Bernhardt, A., Leuendorf, J. E., Drewke, C., Lytovchenko, A., Mujahed, N., Gurgui, C., Frommer, W. B., Leistner, E., Fernie, A. R., and Hellmann, H. (2006) Analysis of the Arabidopsis rsr4-1/pdx1-3 mutant reveals the critical function of the PDX1 protein family in metabolism, development, and vitamin B6 biosynthesis. Plant Cell 18, 1722-1735 (Pubitemid 44025555)
    • (2006) Plant Cell , vol.18 , Issue.7 , pp. 1722-1735
    • Wagner, S.1    Bernhardt, A.2    Leuendorf, J.E.3    Drewke, C.4    Lytovchenko, A.5    Mujahed, N.6    Gurgui, C.7    Frommer, W.B.8    Leistner, E.9    Fernie, A.R.10    Hellmann, H.11
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 34250350465 scopus 로고    scopus 로고
    • Reaction mechanism of pyridoxal 5′-phosphate synthase: Detection of an enzyme-bound chromophoric intermediate
    • DOI 10.1074/jbc.M610614200
    • Raschle, T., Arigoni, D., Brunisholz, R., Rechsteiner, H., Amrhein, N., and Fitzpatrick, T. B. (2007) Reaction mechanism of pyridoxal 5′-phosphate synthase: detection of an enzyme bound chromophoric intermediate. J. Biol. Chem. 282, 6098-6105 (Pubitemid 47100844)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6098-6105
    • Raschle, T.1    Arigoni, D.2    Brunisholz, R.3    Rechsteiner, H.4    Amrhein, N.5    Fitzpatrick, T.B.6
  • 32
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip. A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • Clough, S. J., and Bent, A. F. (1998) Floral dip. A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735-743
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.J.1    Bent, A.F.2
  • 33
    • 84982358134 scopus 로고
    • A revised medium for rapid growth of bioassays with tobacco tissue culture
    • Murashige, T., and Skoog, F. (1962) A revised medium for rapid growth of bioassays with tobacco tissue culture. Physiol. Plant. 15, 473-497
    • (1962) Physiol. Plant. , vol.15 , pp. 473-497
    • Murashige, T.1    Skoog, F.2
  • 34
    • 79251636885 scopus 로고    scopus 로고
    • It takes two to tango. Defining an essential second active site in pyridoxal 5′-phosphate synthase
    • Moccand, C., Kaufmann, M., and Fitzpatrick, T. B. (2011) It takes two to tango. Defining an essential second active site in pyridoxal 5′-phosphate synthase. PLoS One 6, e16042
    • (2011) PLoS One , vol.6
    • Moccand, C.1    Kaufmann, M.2    Fitzpatrick, T.B.3
  • 35
    • 67649340659 scopus 로고    scopus 로고
    • X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases
    • Neuwirth, M., Strohmeier, M., Windeisen, V., Wallner, S., Deller, S., Rippe, K., Sinning, I., Macheroux, P., and Tews, I. (2009) X-ray crystal structure of Saccharomyces cerevisiae Pdx1 provides insights into the oligomeric nature of PLP synthases. FEBS Lett. 583, 2179-2186
    • (2009) FEBS Lett. , vol.583 , pp. 2179-2186
    • Neuwirth, M.1    Strohmeier, M.2    Windeisen, V.3    Wallner, S.4    Deller, S.5    Rippe, K.6    Sinning, I.7    Macheroux, P.8    Tews, I.9
  • 36
    • 65549130157 scopus 로고    scopus 로고
    • Intersubunit cross-talk in pyridoxal 5′-phosphate synthase, coordinated by the C terminus of the synthase subunit
    • Raschle, T., Speziga, D., Kress, W., Moccand, C., Gehrig, P., Amrhein, N., Weber-Ban, E., and Fitzpatrick, T. B. (2009) Intersubunit cross-talk in pyridoxal 5′-phosphate synthase, coordinated by the C terminus of the synthase subunit. J. Biol. Chem. 284, 7706-7718
    • (2009) J. Biol. Chem. , vol.284 , pp. 7706-7718
    • Raschle, T.1    Speziga, D.2    Kress, W.3    Moccand, C.4    Gehrig, P.5    Amrhein, N.6    Weber-Ban, E.7    Fitzpatrick, T.B.8
  • 38
    • 84870329755 scopus 로고    scopus 로고
    • Crystal structure of pyridoxal biosynthesis lyase PdxS from Pyrococcus horikoshii
    • Matsuura, A., Yoon, J. Y., Yoon, H. J., Lee, H. H., and Suh, S. W. (2012) Crystal structure of pyridoxal biosynthesis lyase PdxS from Pyrococcus horikoshii. Mol. Cells 34, 407-412
    • (2012) Mol. Cells , vol.34 , pp. 407-412
    • Matsuura, A.1    Yoon, J.Y.2    Yoon, H.J.3    Lee, H.H.4    Suh, S.W.5
  • 39
    • 41449108267 scopus 로고    scopus 로고
    • Mechanistic studies on pyridoxal phosphate synthase: The reaction pathway leading to a chromophoric intermediate
    • DOI 10.1021/ja076604l
    • Hanes, J. W., Burns, K. E., Hilmey, D. G., Chatterjee, A., Dorrestein, P. C., and Begley, T. P. (2008) Mechanistic studies on pyridoxal phosphate synthase: the reaction pathway leading to a chromophoric intermediate. J. Am. Chem. Soc. 130, 3043-3052 (Pubitemid 351455975)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.10 , pp. 3043-3052
    • Hanes, J.W.1    Burns, K.E.2    Hilmey, D.G.3    Chatterjee, A.4    Dorrestein, P.C.5    Begley, T.P.6
  • 40
    • 41949139157 scopus 로고    scopus 로고
    • Trapping of a chromophoric intermediate in the Pdx1-catalyzed biosynthesis of pyridoxal 5′-phosphate
    • Hanes, J. W., Keresztes, I., and Begley, T. P. (2008) Trapping of a chromophoric intermediate in the Pdx1-catalyzed biosynthesis of pyridoxal 5′-phosphate. Angew. Chem. Int. Ed. Engl. 47, 2102-2105
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 2102-2105
    • Hanes, J.W.1    Keresztes, I.2    Begley, T.P.3
  • 41
    • 45549094803 scopus 로고    scopus 로고
    • 13C NMR snapshots of the complex reaction coordinate of pyridoxal phosphate synthase
    • 13C NMR snapshots of the complex reaction coordinate of pyridoxal phosphate synthase. Nat. Chem. Biol. 4, 425-430
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 425-430
    • Hanes, J.W.1    Keresztes, I.2    Begley, T.P.3
  • 42
    • 0942276237 scopus 로고    scopus 로고
    • Differentiation between peptides containing acetylated or tri-methylated lysines by mass spectrometry: An application for determining lysine 9 acetylation and methylation of histone H3
    • DOI 10.1002/pmic.200300503
    • Zhang, K., Yau, P. M., Chandrasekhar, B., New, R., Kondrat, R., Imai, B. S., and Bradbury, M. E. (2004) Differentiation between peptides containing acetylated or tri-methylated lysines by mass spectrometry: an application for determining lysine 9 acetylation and methylation of histone H3. Proteomics 4, 1-10 (Pubitemid 38140869)
    • (2004) Proteomics , vol.4 , Issue.1 , pp. 1-10
    • Zhang, K.1    Yau, P.M.2    Chandrasekhar, B.3    New, R.4    Kondrat, R.5    Imai, B.S.6    Bradbury, M.E.7
  • 44
    • 79958039807 scopus 로고    scopus 로고
    • Towards a functional understanding of protein N-terminal acetylation
    • Arnesen, T. (2011) Towards a functional understanding of protein N-terminal acetylation. PLoS Biol. 9, e1001074
    • (2011) PLoS Biol. , vol.9
    • Arnesen, T.1
  • 45
    • 84859490749 scopus 로고    scopus 로고
    • Protein N-terminal acetyltransferases: When the start matters
    • Starheim, K. K., Gevaert, K., and Arnesen, T. (2012) Protein N-terminal acetyltransferases: when the start matters. Trends Biochem. Sci. 37, 152-161
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 152-161
    • Starheim, K.K.1    Gevaert, K.2    Arnesen, T.3
  • 46
    • 0037048676 scopus 로고    scopus 로고
    • N-terminal acetylation of ectopic recombinant proteins in Escherichia coli
    • Charbaut, E., Redeker, V., Rossier, J., and Sobel, A. (2002) N-terminal acetylation of ectopic recombinant proteins in Escherichia coli. FEBS Lett. 529, 341-345
    • (2002) FEBS Lett. , vol.529 , pp. 341-345
    • Charbaut, E.1    Redeker, V.2    Rossier, J.3    Sobel, A.4
  • 47
    • 77953880858 scopus 로고    scopus 로고
    • Identification of protein N-terminal methyltransferases in yeast and humans
    • Webb, K. J., Lipson, R. S., Al-Hadid, Q., Whitelegge, J. P., and Clarke, S. G. (2010) Identification of protein N-terminal methyltransferases in yeast and humans. Biochemistry 49, 5225-5235
    • (2010) Biochemistry , vol.49 , pp. 5225-5235
    • Webb, K.J.1    Lipson, R.S.2    Al-Hadid, Q.3    Whitelegge, J.P.4    Clarke, S.G.5
  • 48
    • 0032015703 scopus 로고    scopus 로고
    • SOR1, a gene required for photosensitizer and singlet oxygen resistance in Cercospora fungi, is highly conserved in divergent organisms
    • Ehrenshaft, M., Jenns, A. E., Chung, K. R., and Daub, M. E. (1998) SOR1, a gene required for photosensitizer and singlet oxygen resistance in Cercospora fungi, is highly conserved in divergent organisms. Mol. Cell 1, 603-609 (Pubitemid 128374696)
    • (1998) Molecular Cell , vol.1 , Issue.4 , pp. 603-609
    • Ehrenshaft, M.1    Jenns, A.E.2    Chung, K.R.3    Daub, M.E.4
  • 50
    • 0034978496 scopus 로고    scopus 로고
    • Comprehensive expression profile analysis of the Arabidopsis hsp70 gene family
    • DOI 10.1104/pp.126.2.789
    • Sung, D. Y., Vierling, E., and Guy, C. L. (2001) Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family. Plant Physiol. 126, 789-800 (Pubitemid 32568814)
    • (2001) Plant Physiology , vol.126 , Issue.2 , pp. 789-800
    • Dong, Y.S.1    Vierling, E.2    Guy, C.L.3
  • 54
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER. A unified platform for automated protein structure and function prediction
    • Roy, A., Kucukural, A., and Zhang, Y. (2010) I-TASSER. A unified platform for automated protein structure and function prediction. Nat. Protoc. 5, 725-738
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.