Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves (364 views)
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Apr 1; 67(1): 209-218.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.354, 5-year impact factor: 3.905
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33847399669&partnerID=40&md5=488bd05d9de230aaac9d56c1395edf1d
Keywords: 3d Modelling, Adenine Polynucleotide Glycosylases, Circular Dichroic Spectroscopy, Docking Analysis, Fluorescence Analyses, Ribosome Inactivating Proteins, Complementary Dna, Dna Glycosyltransferase, Polyadenylic Acid, Ribosome Rna, Serine, Unclassified Drug, Article, Catalysis, Enzyme Activity, Enzyme Substrate, Fluorescence Spectroscopy, Molecular Model, Nonhuman, Plant Leaf, Pokeweed, Priority Journal, Protein Purification, Three Dimensional Imaging, Amino Acid Sequence, Animals, Cell-Free System, Cloning, Computer Simulation, Escherichia Coli, Molecular Sequence Data, Mutagenesis, Site-Directed, N-Glycosyl Hydrolases, Phytolacca, Plant Leaves, Plant Proteins, Rabbits, Reticulocytes, Sequence Alignment, Spectrometry, Phytolacca Dioica,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze della Vita, Seconda Università di Napoli, Via Vivaldi 43, I-81100 Caserta, Italy
Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 16, I-80138 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB (Centro di Ricerca Interdipartimentale per le Scienze Computazionali e Biotecnologiche), Seconda Università di Napoli, Via Costantinopoli 16, I-80138 Napoli, Italy
Istituto di Scienze dell'Alimentazione, CNR, Via Roma 52 A/C, 83100 Avellino, Italy
References:
Barbieri, L., Battelli, M.G., Stirpe, F., Ribosome-inactivating proteins from plants (1993) Biochim Biophys Acta, 1154, pp. 237-28
Barbieri, L., Valbonesi, P., Bonora, E., Gorini, P., Bolognesi, A., Stirpe, F., Polynucleotide:adenosine glycosidase activity of ribosome-inactivating proteins: Effect on DNA, RNA and poly(A) (1997) Nucleic Acids Res, 25, pp. 518-522
Bolognesi, A., Polito, L., Lubelli, C., Barbieri, L., Parente, A., Stirpe, F., Ribosome-inactivating and adenine polynucleotide glycosylase activities in Mirabilis jalapa L. tissues (2002) J Biol Chem, 277, pp. 13709-13716
Wang, P., Tumer, N.E., Virus resistance mediated by ribosome inactivating proteins (2000) Adv Virus Res, 55, pp. 325-355
Nielsen, K., Boston, R.S., Ribosome-inactivating proteins: A plant perspective (2001) Annu Rev Plant Physiol Plant Mol Biol, 52, pp. 785-816
Parikh, B.A., Tumer, N.E., Antiviral activity of ribosome inactivating proteins in medicine (2004) Mini Rev Med Chem, 4, pp. 523-543
Hong, Y., Saunders, K., Hartley, M.R., Stanley, J., Resistance to geminivirus infection by virus-induced expression of dianthin in transgenic plants (1996) Virology, 220, pp. 119-127
Lodge, J.K., Kaniewski, W.K., Tumer, N.E., Broad-spectrum virus resistance in transgenic plants expressing pokeweed antiviral protein (1993) Proc Natl Acad Sci USA, 90, pp. 7089-7093
Corrado, G., Delli Bovi, P., Ciliento, R., Gaudio, L., Di Maro, A., Aceto, S., Lorito, M., Rao, R., Inducible expression of a Phytolacca heterotepala ribosome-inactivating protein leads to enhanced resistance against major fungal pathogens in tobacco (2005) Phytopathology, 95, pp. 206-215
Ready, M.P., Kim, Y., Robertus, J.D., Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action (1991) Proteins, 10, pp. 270-278
Katzin, B.J., Collins, E.J., Robertus, J.D., Structure of ricin A-chain at 2.5 A (1991) Proteins, 10, pp. 251-259
Gawlak, S.L., Neubauer, M., Klei, H.E., Chang, C.Y., Einspahr, H.M., Siegall, C.B., Molecular, biological, and preliminary structural analysis of recombinant bryodin 1, a ribosome-inactivating protein from the plant Bryonia dioica (1997) Biochemistry, 36, pp. 3095-3103
Schlossman, D., Withers, D., Welsh, P., Alexander, A., Robertus, J., Frankel, A., Role of glutamic acid 177 of the ricin toxin A chain in enzymatic inactivation of ribosomes (1989) Mol Cell Biol, 9, pp. 5012-5021
Frankel, A., Welsh, P., Richardson, J., Robertus, J.D., Role of arginine 180 and glutamic acid 177 of ricin toxin A chain in enzymatic inactivation of ribosomes (1990) Mol Cell Biol, 10, pp. 6257-6263
Gould, J.H., Hartley, M.R., Welsh, P.C., Hoshizaki, D.K., Frankel, A., Roberts, L.M., Lord, J.M., Alteration of an amino acid residue outside the active site of the ricin A chain reduces its toxicity towards yeast ribosomes (1991) Mol Gen Genet, 230, pp. 81-90
Mlsna, D., Monzingo, A.F., Katzin, B.J., Ernst, S., Robertus, J.D., Structure of recombinant ricin A chain at 2.3 A (1993) Protein Sci, 2, pp. 429-435
Funatsu, G., Islam, M.R., Minami, Y., Sung-Sil, K., Kimura, M., Conserved amino acid residues in ribosome-inactivating proteins from plants (1991) Biochimie, 73, pp. 1157-1161
Di Maro, A., Valbonesi, P., Bolognesi, A., Stirpe, F., De Luca, P., Siniscalco Gigliano, G., Gaudio, L., Parente, A., Isolation and characterization of four type-1 ribosome-inactivating proteins, with polynucleotide:adenosine glycosidase activity, from leaves of Phytolacca dioica L (1999) Planta, 208, pp. 123-131
Sambrook, J., Fritsch, E., Maniatis, T., (1989) Molecular cloning: A laboratory manual, , 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
Del Vecchio Blanco, F., Cafaro, V., Di Maro, A., Scognamiglio, R., Siniscalco, G., Parente, A., Di Donato, A., A recombinant ribosome-inactivating protein from the plant Phytolacca dioica L. produced from a synthetic gene (1998) FEBS Lett, 437, pp. 241-245
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Parente, A., Verde, C., Malorni, A., Montecucchi, P., Aniello, F., Geraci, G., Amino-acid sequence of the cooperative dimeric myoglobin from the radular muscles of the marine gastropod Nassa mutabilis (1993) Biochim Biophys Acta, 1162, pp. 1-9
Johnson, W.J., (1992) Analysis of circular dichroism spectra, pp. 426-447
Johnson, W.J., Protein secondary structure and circular dichroism: A practical guide (1990) Proteins, 7, pp. 205-214
Alston, R.W., Urbanikova, L., Sevcik, J., Lasagna, M., Reinhart, G.D., Scholtz, J.M., Pace, C.N., Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa (2004) Biophys J, 87, pp. 4036-4047
Massiah, A.J., Hartley, M.R., Wheat ribosome-inactivating proteins: Seed and leaf forms with different specificities and cofactor requirements (1995) Planta, 197, pp. 633-640
Parente, A., De Luca, P., Bolognesi, A., Barbieri, L., Battelli, M.G., Abbondanza, A., Sande, M.J., Stirpe, F., Purification and partial characterization of single-chain ribosome-inactivating proteins from the seeds of Phytolacca dioica L (1993) Biochim Biophys Acta, 1216, pp. 43-49
Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W., Lipman, D.J., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Res, 25, pp. 3389-3402
Honjo, E., Dong, D., Motoshima, H., Watanabe, K., Genomic clones encoding two isoforms of pokeweed antiviral protein in seeds (PAP-S1 and S2) and the N-glycosidase activities of their recombinant proteins on ribosomes and DNA in comparison with other isoforms (2002) J Biochem (Tokyo), 131, pp. 225-231
Sali, A., Blundell, T.L., Comparative protein modelling by satisfaction of spatial restraints (1993) J Mol Biol, 234, pp. 779-815
Facchiano, A.M., Stiuso, P., Chiusano, M.L., Caraglia, M., Giuberti, G., Marra, M., Abbruzzese, A., Colonna, G., Homology modelling of the human eukaryotic initiation factor 5A (eIF-5A) (2001) Protein Eng, 14, pp. 881-890
Costantini, S., Rossi, M., Colonna, G., Facchiano, A.M., Modelling of HLA-DQ2 and its interaction with gluten peptides to explain molecular recognition in celiac disease (2005) J Mol Graph Model, 23, pp. 419-431
Scapigliati, G., Costantini, S., Colonna, G., Facchiano, A., Buonocore, F., Bossu, P., Cunningham, C., Secombes, C.J., Modelling of fish interleukin-1 and its receptor (2004) Dev Comp Immunol, 28, pp. 429-441
Buonocore, F., Randelli, E., Bird, S., Secombes, C.J., Costantini, S., Facchiano, A., Mazzini, M., Scapigliati, G., The CD8α from sea bass (Dicentrarchus labrax L.): Cloning, expression and 3D modelling (2006) Fish Shellfish Immunol, 20, pp. 637-646
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Sippl, M.J., Recognition of errors in three-dimensional structures of proteins (1993) Proteins, 17, pp. 355-362
Canutescu, A.A., Shelenkov, A.A., Dunbrack Jr, R.L., A graph-theory algorithm for rapid protein side-chain prediction (2003) Protein Sci, 12, pp. 2001-2014
Dunbrack Jr., R.L., Rotamer libraries in the 21st century (2002) Curr Opin Struct Biol, 12, pp. 431-440
Kabsch, W., Sander, C., Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features (1983) Biopolymers, 22, pp. 2577-2637
Orengo, C.A., Michie, A.D., Jones, S., Jones, D.T., Swindells, M.B., Thornton, J.M., CATH-a hierarchic classification of protein domain structures (1997) Structure, 5, pp. 1093-1108
McDonald, I.K., Thornton, J.M., Satisfying hydrogen bonding potential in proteins (1994) J Mol Biol, 238, pp. 777-793
Wang, Y.X., Neamati, N., Jacob, J., Palmer, I., Stahl, S.J., Kaufman, J.D., Huang, P.L., Torchia, D.A., Solution structure of anti-HIV-1 and anti-tumor protein MAP30: Structural insights into its multiple functions (1999) Cell, 99, pp. 433-442
Wang, Y.X., Jacob, J., Wingfield, P.T., Palmer, I., Stahl, S.J., Kaufman, J.D., Huang, P.L., Torchia, D.A., Anti-HIV and anti-tumor protein MAP30, a 30 kDa single-strand type-I RIP, shares similar secondary structure and beta-sheet topology with the A chain of ricin, a type-II RIP (2000) Protein Sci, 9, pp. 138-144
Tress, M., Ezkurdia, I., Grana, O., Lopez, G., Valencia, A., Assessment of predictions submitted for the CASP6 comparative modeling category (2005) Proteins, 61 (SUPPL. 7), pp. 27-45
Munoz, V., Serrano, L., Elucidating the folding problem of helical peptides using empirical parameters. II. Helix macrodipole effects and rational modification of the helical content of natural peptides (1995) J Mol Biol, 245, pp. 275-296
Facchiano, A.M., Colonna, G., Ragone, R., Helix stabilizing factors and stabilization of thermophilic proteins: An X-ray based study (1998) Protein Eng, 11, pp. 753-760
Endo, Y., Tsurugi, K., RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes (1987) J Biol Chem, 262, pp. 8128-8130
Kurinov, I.V., Myers, D.E., Irvin, J.D., Uckun, F.M., X-ray crystallographic analysis of the structural basis for the interactions of pokeweed antiviral protein with its active site inhibitor and ribosomal RNA substrate analogs (1999) Protein Sci, 8, pp. 1765-1772
Marsden, C.J., Fulop, V., Day, P.J., Lord, J.M., The effect of mutations surrounding and within the active site on the catalytic activity of ricin A chain (2004) Eur J Biochem, 271, pp. 153-162
Robertus, J.D., Monzingo, A.F., The structure of ribosome inactivating proteins (2004) Mini Rev Med Chem, 4, pp. 477-486
Kitaoka, Y., Involvement of the amino acids outside the active-site cleft in the catalysis of ricin A chain (1998) Eur J Biochem, 257, pp. 255-262
Chen, J.K., Hung, C.H., Liaw, Y.C., Lin, J.Y., Identification of amino acid residues of abrin-a A chain is essential for catalysis and reassociation with abrin-a B chain by site-directed mutagenesis (1997) Protein Eng, 10, pp. 827-833
Fryxell, D.K., Gawlak, S.L., Dodge, R.W., Siegall, C.B., Identification of a specific tyrosine residue in Bryodin 1 distinct from the active site but required for full catalytic and cytotoxic activity (1998) Protein Sci, 7, pp. 318-324
Guo, Q., Zhou, W., Too, H.M., Li, J., Liu, Y., Bartlam, M., Dong, Y., Rao, Z., Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants (2003) Protein Eng, 16, pp. 391-396
Parikh, B. A., Tumer, N. E., Antiviral activity of ribosome inactivating proteins in medicine (2004) Mini Rev Med Chem, 4, pp. 523-543
Lodge, J. K., Kaniewski, W. K., Tumer, N. E., Broad-spectrum virus resistance in transgenic plants expressing pokeweed antiviral protein (1993) Proc Natl Acad Sci USA, 90, pp. 7089-7093
Ready, M. P., Kim, Y., Robertus, J. D., Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action (1991) Proteins, 10, pp. 270-278
Katzin, B. J., Collins, E. J., Robertus, J. D., Structure of ricin A-chain at 2. 5 A (1991) Proteins, 10, pp. 251-259
Gawlak, S. L., Neubauer, M., Klei, H. E., Chang, C. Y., Einspahr, H. M., Siegall, C. B., Molecular, biological, and preliminary structural analysis of recombinant bryodin 1, a ribosome-inactivating protein from the plant Bryonia dioica (1997) Biochemistry, 36, pp. 3095-3103
Gould, J. H., Hartley, M. R., Welsh, P. C., Hoshizaki, D. K., Frankel, A., Roberts, L. M., Lord, J. M., Alteration of an amino acid residue outside the active site of the ricin A chain reduces its toxicity towards yeast ribosomes (1991) Mol Gen Genet, 230, pp. 81-90
Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Johnson, W. J., (1992) Analysis of circular dichroism spectra, pp. 426-447
Johnson, W. J., Protein secondary structure and circular dichroism: A practical guide (1990) Proteins, 7, pp. 205-214
Alston, R. W., Urbanikova, L., Sevcik, J., Lasagna, M., Reinhart, G. D., Scholtz, J. M., Pace, C. N., Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa (2004) Biophys J, 87, pp. 4036-4047
Massiah, A. J., Hartley, M. R., Wheat ribosome-inactivating proteins: Seed and leaf forms with different specificities and cofactor requirements (1995) Planta, 197, pp. 633-640
Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., Lipman, D. J., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Res, 25, pp. 3389-3402
Facchiano, A. M., Stiuso, P., Chiusano, M. L., Caraglia, M., Giuberti, G., Marra, M., Abbruzzese, A., Colonna, G., Homology modelling of the human eukaryotic initiation factor 5A (eIF-5A) (2001) Protein Eng, 14, pp. 881-890
Sippl, M. J., Recognition of errors in three-dimensional structures of proteins (1993) Proteins, 17, pp. 355-362
Canutescu, A. A., Shelenkov, A. A., Dunbrack Jr, R. L., A graph-theory algorithm for rapid protein side-chain prediction (2003) Protein Sci, 12, pp. 2001-2014
Dunbrack Jr., R. L., Rotamer libraries in the 21st century (2002) Curr Opin Struct Biol, 12, pp. 431-440
Orengo, C. A., Michie, A. D., Jones, S., Jones, D. T., Swindells, M. B., Thornton, J. M., CATH-a hierarchic classification of protein domain structures (1997) Structure, 5, pp. 1093-1108
McDonald, I. K., Thornton, J. M., Satisfying hydrogen bonding potential in proteins (1994) J Mol Biol, 238, pp. 777-793
Wang, Y. X., Neamati, N., Jacob, J., Palmer, I., Stahl, S. J., Kaufman, J. D., Huang, P. L., Torchia, D. A., Solution structure of anti-HIV-1 and anti-tumor protein MAP30: Structural insights into its multiple functions (1999) Cell, 99, pp. 433-442
Wang, Y. X., Jacob, J., Wingfield, P. T., Palmer, I., Stahl, S. J., Kaufman, J. D., Huang, P. L., Torchia, D. A., Anti-HIV and anti-tumor protein MAP30, a 30 kDa single-strand type-I RIP, shares similar secondary structure and beta-sheet topology with the A chain of ricin, a type-II RIP (2000) Protein Sci, 9, pp. 138-144
Facchiano, A. M., Colonna, G., Ragone, R., Helix stabilizing factors and stabilization of thermophilic proteins: An X-ray based study (1998) Protein Eng, 11, pp. 753-760
Kurinov, I. V., Myers, D. E., Irvin, J. D., Uckun, F. M., X-ray crystallographic analysis of the structural basis for the interactions of pokeweed antiviral protein with its active site inhibitor and ribosomal RNA substrate analogs (1999) Protein Sci, 8, pp. 1765-1772
Marsden, C. J., Fulop, V., Day, P. J., Lord, J. M., The effect of mutations surrounding and within the active site on the catalytic activity of ricin A chain (2004) Eur J Biochem, 271, pp. 153-162
Robertus, J. D., Monzingo, A. F., The structure of ribosome inactivating proteins (2004) Mini Rev Med Chem, 4, pp. 477-486
Chen, J. K., Hung, C. H., Liaw, Y. C., Lin, J. Y., Identification of amino acid residues of abrin-a A chain is essential for catalysis and reassociation with abrin-a B chain by site-directed mutagenesis (1997) Protein Eng, 10, pp. 827-833
Fryxell, D. K., Gawlak, S. L., Dodge, R. W., Siegall, C. B., Identification of a specific tyrosine residue in Bryodin 1 distinct from the active site but required for full catalytic and cytotoxic activity (1998) Protein Sci, 7, pp. 318-324
Proteins (ISSN: 0887-3585, 1097-0134, 1097-0134electronic), 2007 Apr 1; 67(1): 209-218.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.354, 5-year impact factor: 3.905
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-33847399669&partnerID=40&md5=488bd05d9de230aaac9d56c1395edf1d
Keywords: 3d Modelling, Adenine Polynucleotide Glycosylases, Circular Dichroic Spectroscopy, Docking Analysis, Fluorescence Analyses, Ribosome Inactivating Proteins, Complementary Dna, Dna Glycosyltransferase, Polyadenylic Acid, Ribosome Rna, Serine, Unclassified Drug, Article, Catalysis, Enzyme Activity, Enzyme Substrate, Fluorescence Spectroscopy, Molecular Model, Nonhuman, Plant Leaf, Pokeweed, Priority Journal, Protein Purification, Three Dimensional Imaging, Amino Acid Sequence, Animals, Cell-Free System, Cloning, Computer Simulation, Escherichia Coli, Molecular Sequence Data, Mutagenesis, Site-Directed, N-Glycosyl Hydrolases, Phytolacca, Plant Leaves, Plant Proteins, Rabbits, Reticulocytes, Sequence Alignment, Spectrometry, Phytolacca Dioica,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze della Vita, Seconda Università di Napoli, Via Vivaldi 43, I-81100 Caserta, Italy
Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 16, I-80138 Napoli, Italy
Dipartimento di Biochimica e Biofisica, CRISCEB (Centro di Ricerca Interdipartimentale per le Scienze Computazionali e Biotecnologiche), Seconda Università di Napoli, Via Costantinopoli 16, I-80138 Napoli, Italy
Istituto di Scienze dell'Alimentazione, CNR, Via Roma 52 A/C, 83100 Avellino, Italy
References:
Barbieri, L., Battelli, M.G., Stirpe, F., Ribosome-inactivating proteins from plants (1993) Biochim Biophys Acta, 1154, pp. 237-28
Barbieri, L., Valbonesi, P., Bonora, E., Gorini, P., Bolognesi, A., Stirpe, F., Polynucleotide:adenosine glycosidase activity of ribosome-inactivating proteins: Effect on DNA, RNA and poly(A) (1997) Nucleic Acids Res, 25, pp. 518-522
Bolognesi, A., Polito, L., Lubelli, C., Barbieri, L., Parente, A., Stirpe, F., Ribosome-inactivating and adenine polynucleotide glycosylase activities in Mirabilis jalapa L. tissues (2002) J Biol Chem, 277, pp. 13709-13716
Wang, P., Tumer, N.E., Virus resistance mediated by ribosome inactivating proteins (2000) Adv Virus Res, 55, pp. 325-355
Nielsen, K., Boston, R.S., Ribosome-inactivating proteins: A plant perspective (2001) Annu Rev Plant Physiol Plant Mol Biol, 52, pp. 785-816
Parikh, B.A., Tumer, N.E., Antiviral activity of ribosome inactivating proteins in medicine (2004) Mini Rev Med Chem, 4, pp. 523-543
Hong, Y., Saunders, K., Hartley, M.R., Stanley, J., Resistance to geminivirus infection by virus-induced expression of dianthin in transgenic plants (1996) Virology, 220, pp. 119-127
Lodge, J.K., Kaniewski, W.K., Tumer, N.E., Broad-spectrum virus resistance in transgenic plants expressing pokeweed antiviral protein (1993) Proc Natl Acad Sci USA, 90, pp. 7089-7093
Corrado, G., Delli Bovi, P., Ciliento, R., Gaudio, L., Di Maro, A., Aceto, S., Lorito, M., Rao, R., Inducible expression of a Phytolacca heterotepala ribosome-inactivating protein leads to enhanced resistance against major fungal pathogens in tobacco (2005) Phytopathology, 95, pp. 206-215
Ready, M.P., Kim, Y., Robertus, J.D., Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action (1991) Proteins, 10, pp. 270-278
Katzin, B.J., Collins, E.J., Robertus, J.D., Structure of ricin A-chain at 2.5 A (1991) Proteins, 10, pp. 251-259
Gawlak, S.L., Neubauer, M., Klei, H.E., Chang, C.Y., Einspahr, H.M., Siegall, C.B., Molecular, biological, and preliminary structural analysis of recombinant bryodin 1, a ribosome-inactivating protein from the plant Bryonia dioica (1997) Biochemistry, 36, pp. 3095-3103
Schlossman, D., Withers, D., Welsh, P., Alexander, A., Robertus, J., Frankel, A., Role of glutamic acid 177 of the ricin toxin A chain in enzymatic inactivation of ribosomes (1989) Mol Cell Biol, 9, pp. 5012-5021
Frankel, A., Welsh, P., Richardson, J., Robertus, J.D., Role of arginine 180 and glutamic acid 177 of ricin toxin A chain in enzymatic inactivation of ribosomes (1990) Mol Cell Biol, 10, pp. 6257-6263
Gould, J.H., Hartley, M.R., Welsh, P.C., Hoshizaki, D.K., Frankel, A., Roberts, L.M., Lord, J.M., Alteration of an amino acid residue outside the active site of the ricin A chain reduces its toxicity towards yeast ribosomes (1991) Mol Gen Genet, 230, pp. 81-90
Mlsna, D., Monzingo, A.F., Katzin, B.J., Ernst, S., Robertus, J.D., Structure of recombinant ricin A chain at 2.3 A (1993) Protein Sci, 2, pp. 429-435
Funatsu, G., Islam, M.R., Minami, Y., Sung-Sil, K., Kimura, M., Conserved amino acid residues in ribosome-inactivating proteins from plants (1991) Biochimie, 73, pp. 1157-1161
Di Maro, A., Valbonesi, P., Bolognesi, A., Stirpe, F., De Luca, P., Siniscalco Gigliano, G., Gaudio, L., Parente, A., Isolation and characterization of four type-1 ribosome-inactivating proteins, with polynucleotide:adenosine glycosidase activity, from leaves of Phytolacca dioica L (1999) Planta, 208, pp. 123-131
Sambrook, J., Fritsch, E., Maniatis, T., (1989) Molecular cloning: A laboratory manual, , 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory
Del Vecchio Blanco, F., Cafaro, V., Di Maro, A., Scognamiglio, R., Siniscalco, G., Parente, A., Di Donato, A., A recombinant ribosome-inactivating protein from the plant Phytolacca dioica L. produced from a synthetic gene (1998) FEBS Lett, 437, pp. 241-245
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Parente, A., Verde, C., Malorni, A., Montecucchi, P., Aniello, F., Geraci, G., Amino-acid sequence of the cooperative dimeric myoglobin from the radular muscles of the marine gastropod Nassa mutabilis (1993) Biochim Biophys Acta, 1162, pp. 1-9
Johnson, W.J., (1992) Analysis of circular dichroism spectra, pp. 426-447
Johnson, W.J., Protein secondary structure and circular dichroism: A practical guide (1990) Proteins, 7, pp. 205-214
Alston, R.W., Urbanikova, L., Sevcik, J., Lasagna, M., Reinhart, G.D., Scholtz, J.M., Pace, C.N., Contribution of single tryptophan residues to the fluorescence and stability of ribonuclease Sa (2004) Biophys J, 87, pp. 4036-4047
Massiah, A.J., Hartley, M.R., Wheat ribosome-inactivating proteins: Seed and leaf forms with different specificities and cofactor requirements (1995) Planta, 197, pp. 633-640
Parente, A., De Luca, P., Bolognesi, A., Barbieri, L., Battelli, M.G., Abbondanza, A., Sande, M.J., Stirpe, F., Purification and partial characterization of single-chain ribosome-inactivating proteins from the seeds of Phytolacca dioica L (1993) Biochim Biophys Acta, 1216, pp. 43-49
Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W., Lipman, D.J., Gapped BLAST and PSI-BLAST: A new generation of protein database search programs (1997) Nucleic Acids Res, 25, pp. 3389-3402
Honjo, E., Dong, D., Motoshima, H., Watanabe, K., Genomic clones encoding two isoforms of pokeweed antiviral protein in seeds (PAP-S1 and S2) and the N-glycosidase activities of their recombinant proteins on ribosomes and DNA in comparison with other isoforms (2002) J Biochem (Tokyo), 131, pp. 225-231
Sali, A., Blundell, T.L., Comparative protein modelling by satisfaction of spatial restraints (1993) J Mol Biol, 234, pp. 779-815
Facchiano, A.M., Stiuso, P., Chiusano, M.L., Caraglia, M., Giuberti, G., Marra, M., Abbruzzese, A., Colonna, G., Homology modelling of the human eukaryotic initiation factor 5A (eIF-5A) (2001) Protein Eng, 14, pp. 881-890
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Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves
Multiple sequence alignment analysis of ribosome inactivating proteins (RIPs) has revealed the occurrence of an invariant seryl residue in proximity of the catalytic tryptophan. The involvement of this seryl residue in the catalytic mechanism of RIPs was investigated by site-directed mutagenesis in PD-L4, type 1 RIP isolated from Phytolacca dioica leaves. We show that the replacement of Ser211 with Ala apparently does not influence the N-β-glycosidase activity on ribosomes (determined as IC50 in a cell-free system), but it reduces the adenine polynucleotide glycosylase activity (APG), assayed spectrophotometrically on other substrates such as DNA, rRNA, and poly(A). The ability of PDL4 to deadenylate polynucleotides appears more sensitive to the Ser211Ala replacement when poly(A) is used as substrate, as only 33% activity is retained by the mutant, while with more complex and heterogeneous substrates such as DNA and rRNA, its APG activity is 73% and 66%, respectively. While the mutated protein shows a conserved secondary structure by CD, it also exhibits a remarkably enhanced tryptophan fluorescence. This indicates that, although the overall protein tridimensional structure is maintained, removal of the hydrosyl group locally affects the environment of a Trp residue. Modelling and docking analyses confirm the interaction between Ser211 and Trp207, which is located within the active site, thus affecting RIP adenine polynucleotide glycosylase activity. Data accumulated so far confirm the potential involvement of Ser211 in the catalytic mechanism of type 1 RIP PD-L4 and a possible role in stabilizing the conformation of Trp207 side chain, which participates actively in the protein enzymatic activity. © 2007 Wiley-Liss, Inc.
Multiple sequence alignment analysis of ribosome inactivating proteins (RIPs) has revealed the occurrence of an invariant seryl residue in proximity of the catalytic tryptophan. The involvement of this seryl residue in the catalytic mechanism of RIPs was investigated by site-directed mutagenesis in PD-L4, type 1 RIP isolated from Phytolacca dioica leaves. We show that the replacement of Ser211 with Ala apparently does not influence the N-β-glycosidase activity on ribosomes (determined as IC50 in a cell-free system), but it reduces the adenine polynucleotide glycosylase activity (APG), assayed spectrophotometrically on other substrates such as DNA, rRNA, and poly(A). The ability of PDL4 to deadenylate polynucleotides appears more sensitive to the Ser211Ala replacement when poly(A) is used as substrate, as only 33% activity is retained by the mutant, while with more complex and heterogeneous substrates such as DNA and rRNA, its APG activity is 73% and 66%, respectively. While the mutated protein shows a conserved secondary structure by CD, it also exhibits a remarkably enhanced tryptophan fluorescence. This indicates that, although the overall protein tridimensional structure is maintained, removal of the hydrosyl group locally affects the environment of a Trp residue. Modelling and docking analyses confirm the interaction between Ser211 and Trp207, which is located within the active site, thus affecting RIP adenine polynucleotide glycosylase activity. Data accumulated so far confirm the potential involvement of Ser211 in the catalytic mechanism of type 1 RIP PD-L4 and a possible role in stabilizing the conformation of Trp207 side chain, which participates actively in the protein enzymatic activity. © 2007 Wiley-Liss, Inc.
Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves
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Invariant Ser211 is involved in the catalysis of PD-L4, type I RIP from Phytolacca dioica leaves
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Di Maro A, Berisio R, Ruggiero A, Tamburino R, Severino V, Zacchia E, Parente A
* Structural and enzymatic properties of an in vivo proteolytic form of PD-S2, type 1 ribosome-inactivating protein from seeds of Phytolacca dioica (356 views)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2012 May 11; 421(3): 514-520.
Impact Factor: 2.406
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* Structural and enzymatic properties of an in vivo proteolytic form of PD-S2, type 1 ribosome-inactivating protein from seeds of Phytolacca dioica (356 views)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2012 May 11; 421(3): 514-520.
Impact Factor: 2.406
View Export to BibTeX Export to EndNote
1 Records (1 excluding Abstracts).
Total impact factor: 2.406 (2.406 excluding Abstracts).
Total 5 year impact factor: 2.5 (2.5 excluding Abstracts).
Total impact factor: 2.406 (2.406 excluding Abstracts).
Total 5 year impact factor: 2.5 (2.5 excluding Abstracts).
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