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Volumn 413, Issue 3, 2008, Pages 417-427

Insights into the substrate specificity of plant peptide deformylase, an essential enzyme with potential for the development of novel biotechnology applications in agriculture

Author keywords

Actinonin; Arabidopsis; Chloroplast; Co translational; Peptide deformylase; Protein processing

Indexed keywords

ACIDS; AMINES; AMINO ACIDS; BIOTECHNOLOGY; CHROMATOGRAPHIC ANALYSIS; COLLOIDS; ESCHERICHIA COLI; FOOD ADDITIVES; GEL PERMEATION CHROMATOGRAPHY; GELATION; ORGANIC ACIDS; POLYPEPTIDES; POROUS MATERIALS; POWDERS; SUBSTRATES;

EID: 48249100930     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071641     Document Type: Article
Times cited : (13)

References (38)
  • 1
    • 0028053015 scopus 로고
    • Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation
    • Mazel, D., Pochet, S. and Marliere, P. (1994) Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation. EMBO J. 13, 914-923
    • (1994) EMBO J , vol.13 , pp. 914-923
    • Mazel, D.1    Pochet, S.2    Marliere, P.3
  • 2
    • 0034818097 scopus 로고    scopus 로고
    • Eukaryotic peptide deformylases. Nuclear-encoded and chloroplast-targeted enzymes in Arabidopsis
    • Dirk, L. M. A., Williams, M. A. and Houtz, R. L. (2001) Eukaryotic peptide deformylases. Nuclear-encoded and chloroplast-targeted enzymes in Arabidopsis. Plant Physiol. 127, 97-107
    • (2001) Plant Physiol , vol.127 , pp. 97-107
    • Dirk, L.M.A.1    Williams, M.A.2    Houtz, R.L.3
  • 3
    • 0034329475 scopus 로고    scopus 로고
    • Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms
    • Giglione, C., Serero, A., Pierre, M., Boisson, B. and Meinnel, T. (2000) Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms. EMBO J. 19, 5916-5929
    • (2000) EMBO J , vol.19 , pp. 5916-5929
    • Giglione, C.1    Serero, A.2    Pierre, M.3    Boisson, B.4    Meinnel, T.5
  • 4
    • 29644433002 scopus 로고    scopus 로고
    • The crystal structure of mitochondrial (Type 1A) peptide deformylase provides clear guidelines for the design of inhibitors specific for the bacterial forms
    • Fieulaine, S., Juillan-Binard, C., Serero, A., Dardel, F., Giglione, C., Meinnel, T. and Ferrer, J. L. (2005) The crystal structure of mitochondrial (Type 1A) peptide deformylase provides clear guidelines for the design of inhibitors specific for the bacterial forms. J. Biol. Chem. 280, 42315-42324
    • (2005) J. Biol. Chem , vol.280 , pp. 42315-42324
    • Fieulaine, S.1    Juillan-Binard, C.2    Serero, A.3    Dardel, F.4    Giglione, C.5    Meinnel, T.6    Ferrer, J.L.7
  • 6
    • 33748430340 scopus 로고    scopus 로고
    • Peptide deformylase as an antibacterial target: A critical assessment
    • Leeds, J. A. and Dean, C. R. (2006) Peptide deformylase as an antibacterial target: a critical assessment. Curr. Opin. Pharmacol. 6, 445-452
    • (2006) Curr. Opin. Pharmacol , vol.6 , pp. 445-452
    • Leeds, J.A.1    Dean, C.R.2
  • 7
    • 0347993051 scopus 로고    scopus 로고
    • An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway
    • Serero, A., Giglione, C., Sardini, A., Martinez-Sanz, J. and Meinnel, T. (2003) An unusual peptide deformylase features in the human mitochondrial N-terminal methionine excision pathway. J. Biol. Chem. 278, 52953-52963
    • (2003) J. Biol. Chem , vol.278 , pp. 52953-52963
    • Serero, A.1    Giglione, C.2    Sardini, A.3    Martinez-Sanz, J.4    Meinnel, T.5
  • 9
    • 0042473206 scopus 로고    scopus 로고
    • Characterization of a human peptide deformylase: Implications for antibacterial drug design
    • Nguyen, K. T., Hu, X., Colton, C., Chakrabarti, R., Zhu, M. X. and Pei, D. (2003) Characterization of a human peptide deformylase: implications for antibacterial drug design. Biochemistry 42, 9952-9958
    • (2003) Biochemistry , vol.42 , pp. 9952-9958
    • Nguyen, K.T.1    Hu, X.2    Colton, C.3    Chakrabarti, R.4    Zhu, M.X.5    Pei, D.6
  • 10
    • 0031567127 scopus 로고    scopus 로고
    • A survey of polypeptide deformylase function throughout the eubacterial lineage
    • Mazel, D., Coic, E., Blanchard, S., Saurin, W. and Marliere, P. (1997) A survey of polypeptide deformylase function throughout the eubacterial lineage. J. Mol. Biol. 266, 939-949
    • (1997) J. Mol. Biol , vol.266 , pp. 939-949
    • Mazel, D.1    Coic, E.2    Blanchard, S.3    Saurin, W.4    Marliere, P.5
  • 11
    • 0030696625 scopus 로고    scopus 로고
    • Purification, characterization and inhibition of peptide deformylase from Escherichia coli
    • Bajagopalan, P. T., Datta, A. and Pei, D. (1997) Purification, characterization and inhibition of peptide deformylase from Escherichia coli. Biochemistry 36, 13910-13918
    • (1997) Biochemistry , vol.36 , pp. 13910-13918
    • Bajagopalan, P.T.1    Datta, A.2    Pei, D.3
  • 12
    • 33847232619 scopus 로고    scopus 로고
    • Plant peptide deformylase: A novel selectable marker and herbicide target based on essential cotranslational chloroplast protein processing
    • Hou, C. X., Dirk, L. M. A., Pattanaik, S., Das, N. C., Maiti, I. B., Houtz, B. L. and Williams, M. A. (2007) Plant peptide deformylase: a novel selectable marker and herbicide target based on essential cotranslational chloroplast protein processing. Plant Biotechnol. J. 5, 275-281
    • (2007) Plant Biotechnol. J , vol.5 , pp. 275-281
    • Hou, C.X.1    Dirk, L.M.A.2    Pattanaik, S.3    Das, N.C.4    Maiti, I.B.5    Houtz, B.L.6    Williams, M.A.7
  • 13
    • 0037413729 scopus 로고    scopus 로고
    • Control of protein life-span by N-terminal methionine excision
    • Giglione, C., Vallon, O. and Meinnel, T. (2003) Control of protein life-span by N-terminal methionine excision. EMBO J. 22, 13-23
    • (2003) EMBO J , vol.22 , pp. 13-23
    • Giglione, C.1    Vallon, O.2    Meinnel, T.3
  • 14
    • 0036401120 scopus 로고    scopus 로고
    • Specificity of chloroplast-localized peptide deformylases as determined with peptide analogs of chloroplast-translated proteins
    • Dirk, L. M. A., Williams, M. A. and Houtz, R. L. (2002) Specificity of chloroplast-localized peptide deformylases as determined with peptide analogs of chloroplast-translated proteins. Arch. Biochem. Biophys. 406, 135-141
    • (2002) Arch. Biochem. Biophys , vol.406 , pp. 135-141
    • Dirk, L.M.A.1    Williams, M.A.2    Houtz, R.L.3
  • 15
    • 31844455733 scopus 로고    scopus 로고
    • Inhibition of peptide deformylase in Nicotiana tabacum leads to decreased D1 protein accumulation, ultimately resulting in a reduction of photosystem II complexes
    • Hou, C. X., Dirk, L. M. A. and Williams, M. A. (2004) Inhibition of peptide deformylase in Nicotiana tabacum leads to decreased D1 protein accumulation, ultimately resulting in a reduction of photosystem II complexes. Am. J. Bot. 91, 1304-1311
    • (2004) Am. J. Bot , vol.91 , pp. 1304-1311
    • Hou, C.X.1    Dirk, L.M.A.2    Williams, M.A.3
  • 16
    • 33644519967 scopus 로고    scopus 로고
    • The evolution of peptide deformylase as a target: Contribution of biochemistry, genetics and genomics
    • Yuan, Z. and White, R. J. (2006) The evolution of peptide deformylase as a target: contribution of biochemistry, genetics and genomics. Biochem. Pharmacol. 71, 1042-1047
    • (2006) Biochem. Pharmacol , vol.71 , pp. 1042-1047
    • Yuan, Z.1    White, R.J.2
  • 18
    • 0032496227 scopus 로고    scopus 로고
    • Structure of peptide deformylase and identification of the substrate binding site
    • Becker, A., Schlichting, I., Kabsch, W., Schultz, S. and Wagner, A. F. (1998) Structure of peptide deformylase and identification of the substrate binding site. J. Biol. Chem. 273, 11413-11416
    • (1998) J. Biol. Chem , vol.273 , pp. 11413-11416
    • Becker, A.1    Schlichting, I.2    Kabsch, W.3    Schultz, S.4    Wagner, A.F.5
  • 19
    • 0030694781 scopus 로고    scopus 로고
    • Crystal structure of the Escherichia coli peptide deformylase
    • Chan, M. K., Gong, W., Rajagopalan, P. T., Hao, B., Tsai, C. M. and Pei, D. (1997) Crystal structure of the Escherichia coli peptide deformylase. Biochemistry 36, 13904-13909
    • (1997) Biochemistry , vol.36 , pp. 13904-13909
    • Chan, M.K.1    Gong, W.2    Rajagopalan, P.T.3    Hao, B.4    Tsai, C.M.5    Pei, D.6
  • 20
    • 0030603915 scopus 로고    scopus 로고
    • A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase
    • Meinnel, T., Blanquet, S. and Dardel, F. (1996) A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase. J. Mol. Biol. 262, 375-386
    • (1996) J. Mol. Biol , vol.262 , pp. 375-386
    • Meinnel, T.1    Blanquet, S.2    Dardel, F.3
  • 21
    • 0036124280 scopus 로고    scopus 로고
    • Crystals of peptide deformylase from Plasmodium falciparum reveal critical characteristics of the active site for drug design
    • Kumar, A., Nguyen, K. T., Srivathsan, S., Ornstein, B., Turley, S., Hirsh, I., Pei, D. and Hol, W. G. (2002) Crystals of peptide deformylase from Plasmodium falciparum reveal critical characteristics of the active site for drug design. Structure 10, 357-367
    • (2002) Structure , vol.10 , pp. 357-367
    • Kumar, A.1    Nguyen, K.T.2    Srivathsan, S.3    Ornstein, B.4    Turley, S.5    Hirsh, I.6    Pei, D.7    Hol, W.G.8
  • 22
    • 0031571098 scopus 로고    scopus 로고
    • Continuous spectrophotometric assay of peptide deformylase
    • Wei, Y. and Pei, D. (1997) Continuous spectrophotometric assay of peptide deformylase. Anal. Biochem. 250, 29-34
    • (1997) Anal. Biochem , vol.250 , pp. 29-34
    • Wei, Y.1    Pei, D.2
  • 23
    • 0031059783 scopus 로고    scopus 로고
    • Practical cryocrystallography
    • Rodgers, D. W. (1997) Practical cryocrystallography. Methods Enzymol. 276, 183-203
    • (1997) Methods Enzymol , vol.276 , pp. 183-203
    • Rodgers, D.W.1
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W. and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 27
    • 0026319199 scopus 로고    scopus 로고
    • Nicholls, A., Sharp, K. A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 281-296
    • Nicholls, A., Sharp, K. A. and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 281-296
  • 29
    • 0029878720 scopus 로고    scopus 로고
    • Humphrey, W., Dalke, A. and Schulten, K. (1996) VMD: Visual Molecular Dynamics. J. Mol. Graph. 14, 33-38
    • Humphrey, W., Dalke, A. and Schulten, K. (1996) VMD: Visual Molecular Dynamics. J. Mol. Graph. 14, 33-38
  • 31
    • 29644438077 scopus 로고    scopus 로고
    • Novel conformational states of peptide deformylase from pathogenic bacterium Leptospira interrogans: Implications for population shift
    • Zhou, Z., Song, X. and Gong, W. (2005) Novel conformational states of peptide deformylase from pathogenic bacterium Leptospira interrogans: implications for population shift. J. Biol. Chem. 280, 42391-42396
    • (2005) J. Biol. Chem , vol.280 , pp. 42391-42396
    • Zhou, Z.1    Song, X.2    Gong, W.3
  • 32
    • 0033547751 scopus 로고    scopus 로고
    • Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library
    • Hu, Y. J., Wei, Y., Zhou, Y., Rajagopalan, P. T. and Pei, D. (1999) Determination of substrate specificity for peptide deformylase through the screening of a combinatorial peptide library. Biochemistry 38, 643-650
    • (1999) Biochemistry , vol.38 , pp. 643-650
    • Hu, Y.J.1    Wei, Y.2    Zhou, Y.3    Rajagopalan, P.T.4    Pei, D.5
  • 33
    • 9444266430 scopus 로고    scopus 로고
    • The apicoplast: A review of the derived plastid of apicomplexan parasites
    • Waller, R. F. and McFadden, G. I. (2005) The apicoplast: a review of the derived plastid of apicomplexan parasites. Curr. Issues Mol. Biol. 7, 57-79
    • (2005) Curr. Issues Mol. Biol , vol.7 , pp. 57-79
    • Waller, R.F.1    McFadden, G.I.2
  • 34
    • 0035824874 scopus 로고    scopus 로고
    • Distinctive features of the two classes of eukaryotic peptide deformylases
    • Serero, A., Giglione, C. and Meinnel, T. (2001) Distinctive features of the two classes of eukaryotic peptide deformylases. J. Mol. Biol. 314, 695-708
    • (2001) J. Mol. Biol , vol.314 , pp. 695-708
    • Serero, A.1    Giglione, C.2    Meinnel, T.3
  • 35
    • 0033528708 scopus 로고    scopus 로고
    • Design and synthesis of substrate analogue inhibitors of peptide deformylase
    • Meinnel, T., Patiny, L., Ragusa, S. and Blanquet, S. (1999) Design and synthesis of substrate analogue inhibitors of peptide deformylase. Biochemistry 38, 4287-4295
    • (1999) Biochemistry , vol.38 , pp. 4287-4295
    • Meinnel, T.1    Patiny, L.2    Ragusa, S.3    Blanquet, S.4
  • 36
    • 0033603628 scopus 로고    scopus 로고
    • Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin
    • Ragusa, S., Mouchet, P., Lazennec, C., Dive, V. and Meinnel, T. (1999) Substrate recognition and selectivity of peptide deformylase. Similarities and differences with metzincins and thermolysin. J. Mol. Biol. 289, 1445-1457
    • (1999) J. Mol. Biol , vol.289 , pp. 1445-1457
    • Ragusa, S.1    Mouchet, P.2    Lazennec, C.3    Dive, V.4    Meinnel, T.5
  • 37
    • 0035543404 scopus 로고    scopus 로고
    • Organellar peptide deformylases: Universality of the N-terminal methionine cleavage mechanism
    • Giglione, C. and Meinnel, T. (2001) Organellar peptide deformylases: universality of the N-terminal methionine cleavage mechanism. Trends Plant Sci. 6, 566-572
    • (2001) Trends Plant Sci , vol.6 , pp. 566-572
    • Giglione, C.1    Meinnel, T.2
  • 38
    • 0030221022 scopus 로고    scopus 로고
    • Degradation pattern of photosystem II reaction center protein D1 in intact leaves. The major photoinhibition-induced cleavage site in D1 polypeptide is located amino terminally of the DE loop
    • Kettunen, R., Tyystjarvi, E. and Aro, E. M. (1996) Degradation pattern of photosystem II reaction center protein D1 in intact leaves. The major photoinhibition-induced cleavage site in D1 polypeptide is located amino terminally of the DE loop. Plant Physiol. 111, 1183-1190
    • (1996) Plant Physiol , vol.111 , pp. 1183-1190
    • Kettunen, R.1    Tyystjarvi, E.2    Aro, E.M.3


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