Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts (340 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2011; 15(2): 259-270.
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Paper type: Journal Article,
Impact factor: 2.941, 5-year impact factor: 2.565
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79952244559&partnerID=40&md5=a775aa8e574f75d1010ffedcdf6cbbed
Keywords: Deinococcus Radiodurans, Extremophiles, Gamma-Glutamyltranspeptidases, Molecular Adaptation, Thermus Thermophilus, Gamma Glutamyltransferase, Glutamine, Glutathione, Recombinant Protein, Amino Acid Sequence, Article, Chemistry, Enzymology, Genetics, Hydrolysis, Metabolism, Molecular Cloning, Molecular Genetics, Phylogeny, Plasmid, Protein Conformation, Protein Tertiary Structure, Sequence Homology, Temperature, Gamma-Glutamyltransferase, Hydrogen-Ion Concentration, Molecular Sequence Data, Protein Structure, Bacteria (microorganisms), Eukaryota, Geobacillus, Geobacillus Thermodenitrificans,
Affiliations:
*** IBB - CNR ***
CNR, Institute of Protein Biochemistry, via Pietro Castellino 111, 80131 Naples, Italy
Department of Chemistry, University of Naples 'Federico II', via Cintia, 80126 Naples, Italy
References:
Boanca, G., Sand, A., Barycki, J.J., Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori gamma-glutamyltranspeptidase (2006) J Biol Chem, 281, pp. 19029-1903
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal Biochem, 72, pp. 248-254
Bryson, K., McGuffin, L.J., Marsden, R.L., Ward, J.J., Sodhi, J.S., Jones, D.T., Protein structure prediction servers at University College London (2005) Nucl Acids Res, 33, pp. W36-W38. , (Web Server issue)
Castellano, I., Merlino, A., Rossi, M., la Cara, F., Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: an enzyme specialized in hydrolase activity (2010) Biochimie, 92, pp. 464-474
de Vendittis, E., Castellano, I., Cotugno, R., Ruocco, M.R., Raimo, G., Masullo, M., Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition (2008) J Theor Biol, 250, pp. 156-171
Emdin, M., Pompella, A., Paolicchi, A., Gamma-glutamyltransferase, atherosclerosis, and cardiovascular disease: triggering oxidative stress within the plaque (2005) Circulation, 112, pp. 2130-2137
Henne, A., Brüggemann, H., Raasch, C., Wiezer, A., Hartsch, T., Liesegang, H., Johann, A., Fritz, H.J., The genome sequence of the extreme thermophile Thermus thermophilus (2004) Nat Biotechnol, 22, pp. 547-553
Ikeda, Y., Fujii, J., Anderson, M.E., Taniguchi, N., Meister, A., Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase (1995) J Biol Chem, 270, pp. 22223-22228
Jones, T.A., Bergdoll, M., Kjeldgaard, M., O: a macromolecular modeling environment (1990) Crystallographic and Modeling Methods in Molecular Design, pp. 189-195. , C. Bugg and S. Ealick (Eds.), Berlin: Springer
Kinlough, C.L., Poland, P.A., Bruns, J.B., Hughey, R.P., Gamma-glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum (2005) Methods Enzymol, 401, pp. 426-449
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Larkin, M.A., Blackshields, G., Brown, N.P., Chenna, R., McGettigan, P.A., McWilliam, H., Valentin, F., Higgins, D.G., Clustal W and Clustal X version 2.0 (2007) Bioinformatics, 23, pp. 2947-2948
Lin, L.L., Chou, P.R., Hua, Y.W., Hsu, W.H., Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacilluslicheniformis (2006) Appl Microbiol Biotechnol, 73, pp. 103-112
Lyu, R.C., Hu, H.Y., Kuo, L.Y., Lo, H.F., Ong, P.L., Chang, H.P., Lin, L.L., Role of the conserved Thr399 and Thr417 residues of Bacillus licheniformis gamma-Glutamyltranspeptidase as evaluated by mutational analysis (2009) Curr Microbiol, 59, pp. 101-106
McDonald, I.K., Thornton, J.M., Satisfying hydrogen bonding potential in proteins (1994) J Mol Biol, 238, pp. 777-793
Minami, H., Suzuki, H., Kumagai, H., A mutant Bacillus subtilis gamma-glutamyltranspeptidase specialized in hydrolysis activity (2003) FEMS Microbiol Lett, 224, pp. 169-173
Okada, T., Suzuki, H., Wada, K., Kumagai, H., Fukuyama, K., Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate (2006) Proc Natl Acad Sci USA, 103, pp. 6471-6476
Pompella, A., Corti, A., Paolicchi, A., Giommarelli, C., Zunino, F., Gamma-glutamyltransferase, redox regulation and cancer drug resistance (2007) Curr Opin Pharmacol, 7, pp. 360-366
Ruepp, A., Graml, W., Santos-Martinez, M.L., Koretke, K.K., Volker, C., Mewes, H.W., Frishman, D., Baumeister, W., The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum (2000) Nature, 407, pp. 508-513
Suzuki, H., Yamada, C., Kato, K., Gamma-glutamyl compounds and their enzymatic production using bacterial gamma-glutamyltranspeptidase (2007) Amino Acids, 32, pp. 333-340
Szilagyi, A., Zavodsky, P., Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey (2000) Struct Fold Des, 8, pp. 493-504
Takami, H., Nakasone, K., Takaki, Y., Maeno, G., Sasaki, R., Masui, N., Fuji, F., Horikoshi, K., Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis (2000) Nucleic Acids Res, 28, pp. 4317-4331
Tate, S.S., Meister, A., Gamma-Glutamyl transpeptidase: catalytic, structural and functional aspects (1981) Mol Cell Biochem, 39, pp. 357-368
van der Spoel, D., van Druner, R., Berendsen, H.J.C., (1994) GROningen MAchine for Chemical Simulation, , Groningen: Department of Biophysical Chemistry, BIOSON Research Institute
Vermeulen, N., Gänzle, M.G., Vogel, R.F., Glutamine deamidation by cereal-associated lactic acid bacteria (2007) J Appl Microbiol, 103, pp. 1197-1205
Wada, K., Irie, M., Suzuki, H., Fukuyama, K., Crystal structure of the halotolerant gamma-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket (2010) FEBS J, 277, pp. 1000-1009
White, O., Eisen, J.A., Heidelberg, J.F., Hickey, E.K., Peterson, J.D., Dodson, R.J., Haft, D.H., Fraser, C.M., Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1 (1999) Science, 286, pp. 1571-1577
Wiederstein, M., Sippl, M.J., ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins (2007) Nucleic Acids Res, 35, pp. 407-410
Willard, L., Ranjan, A., Zhang, H., Monzavi, H., Boyko, R.F., Sykes, B.D., Wishart, D.S., VADAR: a web server for quantitative evaluation of protein structure quality (2003) Nucleic Acids Res, 31, pp. 3316-3319
Williams, K., Cullati, S., Sand, A., Biterova, E.I., Barycki, J.J., Crystal structure of acivicin-inhibited γ-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis (2009) Biochemistry, 48, pp. 2459-2467
Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal Biochem, 72, pp. 248-254
Henne, A., Br ggemann, H., Raasch, C., Wiezer, A., Hartsch, T., Liesegang, H., Johann, A., Fritz, H. J., The genome sequence of the extreme thermophile Thermus thermophilus (2004) Nat Biotechnol, 22, pp. 547-553
Jones, T. A., Bergdoll, M., Kjeldgaard, M., O: a macromolecular modeling environment (1990) Crystallographic and Modeling Methods in Molecular Design, pp. 189-195. , C. Bugg and S. Ealick (Eds.), Berlin: Springer
Kinlough, C. L., Poland, P. A., Bruns, J. B., Hughey, R. P., Gamma-glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum (2005) Methods Enzymol, 401, pp. 426-449
Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., McWilliam, H., Valentin, F., Higgins, D. G., Clustal W and Clustal X version 2. 0 (2007) Bioinformatics, 23, pp. 2947-2948
Lin, L. L., Chou, P. R., Hua, Y. W., Hsu, W. H., Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacilluslicheniformis (2006) Appl Microbiol Biotechnol, 73, pp. 103-112
Lyu, R. C., Hu, H. Y., Kuo, L. Y., Lo, H. F., Ong, P. L., Chang, H. P., Lin, L. L., Role of the conserved Thr399 and Thr417 residues of Bacillus licheniformis gamma-Glutamyltranspeptidase as evaluated by mutational analysis (2009) Curr Microbiol, 59, pp. 101-106
McDonald, I. K., Thornton, J. M., Satisfying hydrogen bonding potential in proteins (1994) J Mol Biol, 238, pp. 777-793
Tate, S. S., Meister, A., Gamma-Glutamyl transpeptidase: catalytic, structural and functional aspects (1981) Mol Cell Biochem, 39, pp. 357-368
Vermeulen, N., G nzle, M. G., Vogel, R. F., Glutamine deamidation by cereal-associated lactic acid bacteria (2007) J Appl Microbiol, 103, pp. 1197-1205
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2011; 15(2): 259-270.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 2.941, 5-year impact factor: 2.565
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79952244559&partnerID=40&md5=a775aa8e574f75d1010ffedcdf6cbbed
Keywords: Deinococcus Radiodurans, Extremophiles, Gamma-Glutamyltranspeptidases, Molecular Adaptation, Thermus Thermophilus, Gamma Glutamyltransferase, Glutamine, Glutathione, Recombinant Protein, Amino Acid Sequence, Article, Chemistry, Enzymology, Genetics, Hydrolysis, Metabolism, Molecular Cloning, Molecular Genetics, Phylogeny, Plasmid, Protein Conformation, Protein Tertiary Structure, Sequence Homology, Temperature, Gamma-Glutamyltransferase, Hydrogen-Ion Concentration, Molecular Sequence Data, Protein Structure, Bacteria (microorganisms), Eukaryota, Geobacillus, Geobacillus Thermodenitrificans,
Affiliations:
*** IBB - CNR ***
CNR, Institute of Protein Biochemistry, via Pietro Castellino 111, 80131 Naples, Italy
Department of Chemistry, University of Naples 'Federico II', via Cintia, 80126 Naples, Italy
References:
Boanca, G., Sand, A., Barycki, J.J., Uncoupling the enzymatic and autoprocessing activities of Helicobacter pylori gamma-glutamyltranspeptidase (2006) J Biol Chem, 281, pp. 19029-1903
Bradford, M.M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal Biochem, 72, pp. 248-254
Bryson, K., McGuffin, L.J., Marsden, R.L., Ward, J.J., Sodhi, J.S., Jones, D.T., Protein structure prediction servers at University College London (2005) Nucl Acids Res, 33, pp. W36-W38. , (Web Server issue)
Castellano, I., Merlino, A., Rossi, M., la Cara, F., Biochemical and structural properties of gamma-glutamyl transpeptidase from Geobacillus thermodenitrificans: an enzyme specialized in hydrolase activity (2010) Biochimie, 92, pp. 464-474
de Vendittis, E., Castellano, I., Cotugno, R., Ruocco, M.R., Raimo, G., Masullo, M., Adaptation of model proteins from cold to hot environments involves continuous and small adjustments of average parameters related to amino acid composition (2008) J Theor Biol, 250, pp. 156-171
Emdin, M., Pompella, A., Paolicchi, A., Gamma-glutamyltransferase, atherosclerosis, and cardiovascular disease: triggering oxidative stress within the plaque (2005) Circulation, 112, pp. 2130-2137
Henne, A., Brüggemann, H., Raasch, C., Wiezer, A., Hartsch, T., Liesegang, H., Johann, A., Fritz, H.J., The genome sequence of the extreme thermophile Thermus thermophilus (2004) Nat Biotechnol, 22, pp. 547-553
Ikeda, Y., Fujii, J., Anderson, M.E., Taniguchi, N., Meister, A., Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase (1995) J Biol Chem, 270, pp. 22223-22228
Jones, T.A., Bergdoll, M., Kjeldgaard, M., O: a macromolecular modeling environment (1990) Crystallographic and Modeling Methods in Molecular Design, pp. 189-195. , C. Bugg and S. Ealick (Eds.), Berlin: Springer
Kinlough, C.L., Poland, P.A., Bruns, J.B., Hughey, R.P., Gamma-glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum (2005) Methods Enzymol, 401, pp. 426-449
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Larkin, M.A., Blackshields, G., Brown, N.P., Chenna, R., McGettigan, P.A., McWilliam, H., Valentin, F., Higgins, D.G., Clustal W and Clustal X version 2.0 (2007) Bioinformatics, 23, pp. 2947-2948
Lin, L.L., Chou, P.R., Hua, Y.W., Hsu, W.H., Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacilluslicheniformis (2006) Appl Microbiol Biotechnol, 73, pp. 103-112
Lyu, R.C., Hu, H.Y., Kuo, L.Y., Lo, H.F., Ong, P.L., Chang, H.P., Lin, L.L., Role of the conserved Thr399 and Thr417 residues of Bacillus licheniformis gamma-Glutamyltranspeptidase as evaluated by mutational analysis (2009) Curr Microbiol, 59, pp. 101-106
McDonald, I.K., Thornton, J.M., Satisfying hydrogen bonding potential in proteins (1994) J Mol Biol, 238, pp. 777-793
Minami, H., Suzuki, H., Kumagai, H., A mutant Bacillus subtilis gamma-glutamyltranspeptidase specialized in hydrolysis activity (2003) FEMS Microbiol Lett, 224, pp. 169-173
Okada, T., Suzuki, H., Wada, K., Kumagai, H., Fukuyama, K., Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate (2006) Proc Natl Acad Sci USA, 103, pp. 6471-6476
Pompella, A., Corti, A., Paolicchi, A., Giommarelli, C., Zunino, F., Gamma-glutamyltransferase, redox regulation and cancer drug resistance (2007) Curr Opin Pharmacol, 7, pp. 360-366
Ruepp, A., Graml, W., Santos-Martinez, M.L., Koretke, K.K., Volker, C., Mewes, H.W., Frishman, D., Baumeister, W., The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum (2000) Nature, 407, pp. 508-513
Suzuki, H., Yamada, C., Kato, K., Gamma-glutamyl compounds and their enzymatic production using bacterial gamma-glutamyltranspeptidase (2007) Amino Acids, 32, pp. 333-340
Szilagyi, A., Zavodsky, P., Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey (2000) Struct Fold Des, 8, pp. 493-504
Takami, H., Nakasone, K., Takaki, Y., Maeno, G., Sasaki, R., Masui, N., Fuji, F., Horikoshi, K., Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis (2000) Nucleic Acids Res, 28, pp. 4317-4331
Tate, S.S., Meister, A., Gamma-Glutamyl transpeptidase: catalytic, structural and functional aspects (1981) Mol Cell Biochem, 39, pp. 357-368
van der Spoel, D., van Druner, R., Berendsen, H.J.C., (1994) GROningen MAchine for Chemical Simulation, , Groningen: Department of Biophysical Chemistry, BIOSON Research Institute
Vermeulen, N., Gänzle, M.G., Vogel, R.F., Glutamine deamidation by cereal-associated lactic acid bacteria (2007) J Appl Microbiol, 103, pp. 1197-1205
Wada, K., Irie, M., Suzuki, H., Fukuyama, K., Crystal structure of the halotolerant gamma-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket (2010) FEBS J, 277, pp. 1000-1009
White, O., Eisen, J.A., Heidelberg, J.F., Hickey, E.K., Peterson, J.D., Dodson, R.J., Haft, D.H., Fraser, C.M., Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1 (1999) Science, 286, pp. 1571-1577
Wiederstein, M., Sippl, M.J., ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins (2007) Nucleic Acids Res, 35, pp. 407-410
Willard, L., Ranjan, A., Zhang, H., Monzavi, H., Boyko, R.F., Sykes, B.D., Wishart, D.S., VADAR: a web server for quantitative evaluation of protein structure quality (2003) Nucleic Acids Res, 31, pp. 3316-3319
Williams, K., Cullati, S., Sand, A., Biterova, E.I., Barycki, J.J., Crystal structure of acivicin-inhibited γ-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis (2009) Biochemistry, 48, pp. 2459-2467
Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding (1976) Anal Biochem, 72, pp. 248-254
Henne, A., Br ggemann, H., Raasch, C., Wiezer, A., Hartsch, T., Liesegang, H., Johann, A., Fritz, H. J., The genome sequence of the extreme thermophile Thermus thermophilus (2004) Nat Biotechnol, 22, pp. 547-553
Jones, T. A., Bergdoll, M., Kjeldgaard, M., O: a macromolecular modeling environment (1990) Crystallographic and Modeling Methods in Molecular Design, pp. 189-195. , C. Bugg and S. Ealick (Eds.), Berlin: Springer
Kinlough, C. L., Poland, P. A., Bruns, J. B., Hughey, R. P., Gamma-glutamyltranspeptidase: disulfide bridges, propeptide cleavage, and activation in the endoplasmic reticulum (2005) Methods Enzymol, 401, pp. 426-449
Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature, 227, pp. 680-685
Larkin, M. A., Blackshields, G., Brown, N. P., Chenna, R., McGettigan, P. A., McWilliam, H., Valentin, F., Higgins, D. G., Clustal W and Clustal X version 2. 0 (2007) Bioinformatics, 23, pp. 2947-2948
Lin, L. L., Chou, P. R., Hua, Y. W., Hsu, W. H., Overexpression, one-step purification, and biochemical characterization of a recombinant gamma-glutamyltranspeptidase from Bacilluslicheniformis (2006) Appl Microbiol Biotechnol, 73, pp. 103-112
Lyu, R. C., Hu, H. Y., Kuo, L. Y., Lo, H. F., Ong, P. L., Chang, H. P., Lin, L. L., Role of the conserved Thr399 and Thr417 residues of Bacillus licheniformis gamma-Glutamyltranspeptidase as evaluated by mutational analysis (2009) Curr Microbiol, 59, pp. 101-106
McDonald, I. K., Thornton, J. M., Satisfying hydrogen bonding potential in proteins (1994) J Mol Biol, 238, pp. 777-793
Tate, S. S., Meister, A., Gamma-Glutamyl transpeptidase: catalytic, structural and functional aspects (1981) Mol Cell Biochem, 39, pp. 357-368
Vermeulen, N., G nzle, M. G., Vogel, R. F., Glutamine deamidation by cereal-associated lactic acid bacteria (2007) J Appl Microbiol, 103, pp. 1197-1205
Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts
γ-Glutamyltranspeptidase (γ-GT) is an ubiquitous enzyme that catalyzes the hydrolysis of γ-glutamyl bonds in glutathione and glutamine and the transfer of the released γ-glutamyl group to amino acids or short peptides. γ-GTs from extremophiles, bacteria adapted to live in hostile environments, were selected as model systems to study the molecular underpinnings of their adaptation to extreme conditions and to find out special properties of potential biotechnological interest. Here, we report the cloning, expression and purification of two members of γ-GT family from two different extremophilic species, Thermus thermophilus (TtGT) and Deinococcus radiodurans (DrGT); the first is an aerobic eubacterium, growing at high temperatures (50-82°C), the second is a polyextremophile, as it tolerates radiations, cold, dehydration, vacuum, and acid. TtGT and DrGT were both synthesized as precursor proteins of 59-60kDa, undergoing an intramolecular auto-cleavage to yield two subunits of 40 and 19-20kDa, respectively. However, like the γ-GT from Geobacillus thermodenitrificans, but differently from the other characterized bacterial and eukaryotic γ-GTs, the two new extremophilic enzymes displayed γ-glutamyl hydrolase, but not transpeptidase activity in the 37-50°C temperature range, pH 8.0. The comparison of sequences and structural models of these two proteins with experimental-determined structures of other known mesophilic γ-GTs suggests that the extremophilic members of this protein family have found a common strategy to adapt to different hostile environments. Moreover, a phylogenetic analysis suggests that γ-GTs displaying only γ-glutamyl hydrolase activity could represent the progenitors of the bacterial and eukaryotic counterparts. © 2011 Springer.
γ-Glutamyltranspeptidase (γ-GT) is an ubiquitous enzyme that catalyzes the hydrolysis of γ-glutamyl bonds in glutathione and glutamine and the transfer of the released γ-glutamyl group to amino acids or short peptides. γ-GTs from extremophiles, bacteria adapted to live in hostile environments, were selected as model systems to study the molecular underpinnings of their adaptation to extreme conditions and to find out special properties of potential biotechnological interest. Here, we report the cloning, expression and purification of two members of γ-GT family from two different extremophilic species, Thermus thermophilus (TtGT) and Deinococcus radiodurans (DrGT); the first is an aerobic eubacterium, growing at high temperatures (50-82°C), the second is a polyextremophile, as it tolerates radiations, cold, dehydration, vacuum, and acid. TtGT and DrGT were both synthesized as precursor proteins of 59-60kDa, undergoing an intramolecular auto-cleavage to yield two subunits of 40 and 19-20kDa, respectively. However, like the γ-GT from Geobacillus thermodenitrificans, but differently from the other characterized bacterial and eukaryotic γ-GTs, the two new extremophilic enzymes displayed γ-glutamyl hydrolase, but not transpeptidase activity in the 37-50°C temperature range, pH 8.0. The comparison of sequences and structural models of these two proteins with experimental-determined structures of other known mesophilic γ-GTs suggests that the extremophilic members of this protein family have found a common strategy to adapt to different hostile environments. Moreover, a phylogenetic analysis suggests that γ-GTs displaying only γ-glutamyl hydrolase activity could represent the progenitors of the bacterial and eukaryotic counterparts. © 2011 Springer.
Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts
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Gene cloning and protein expression of γ-glutamyltranspeptidases from Thermus thermophilus and Deinococcus radiodurans: Comparison of molecular and structural properties with mesophilic counterparts
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Berisio R, Schluenzen F, Harms J, Bashan A, Auerbach T, Baram D, Yonath A
* Structural insight into the role of the ribosomal tunnel in cellular regulation (375 views)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Impact Factor: 11.579
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Bashan A, Agmon I, Zarivach R, Schluenzen F, Harms J, Berisio R, Bartels H, Franceschi F, Auerbach T, Hansen HAS, Kossoy E, Kessler M, Yonath A
* Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression (461 views)
Mol Cell (ISSN: 1097-2765, 1097-4164), 2003 Jan; 11(1): 91-102.
Impact Factor: 16.835
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* A physicochemical investigation on the metal binding properties of TtSmtB, a thermophilic member of the ArsR/SmtB transcription factor family (196 views)
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2019 Jul 26; 138: 1056-1063.
Impact Factor: 4.784
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Aulitto M, Fusco S, Fiorentino G, Limauro D, Pedone E, Bartolucci S, Contursi P
* Thermus thermophilus as source of thermozymes for biotechnologicalapplications: homologous expression and biochemical characterization of anα-galactosidase (214 views) (PDF 173 views)
Microbial Cell Fact, 2017 Feb; N/D: N/D-N/D.
Impact Factor: 3.681
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Pedone E, Fiorentino G, Pirone L, Contursi P, Bartolucci S, Limauro D
* Functional and structural characterization of protein disulfide oxidoreductase from Thermus thermophilus HB27 (343 views)
Extremophiles (ISSN: 1431-0651, 1433-4909, 1433-4909electronic), 2014 Jul; 18(4): 723-731.
Impact Factor: 2.306
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Del Giudice I, Limauro D, Pedone E, Bartolucci S, Fiorentino G
* A novel arsenate reductase from the bacterium Thermus thermophilus HB27: Its role in arsenic detoxification (420 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2013 Oct; 1834(10): 2071-2079.
Impact Factor: 3.191
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Pica A, Russo Krauss I, Castellano I, Rossi M, La Cara F, Graziano G, Sica F, Merlino A
* Exploring The Unfolding Mechanism Of Gamma-Glutamyltranspeptidases: The Case Of The Thermophilic Enzyme From Geobacillus Thermodenitrificans (422 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2012 Apr; 1824(4): 571-577.
Impact Factor: 3.733
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Pennacchio A, Giordano A, Esposito L, Langella E, Rossi M, Raia CA
* Insight into the stereospecificity of short-chain Thermus thermophilus alcohol dehydrogenase showing pro-S hydride transfer and Prelog enantioselectivity (453 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2010 Apr; 17(4): 437-443.
Impact Factor: 1.849
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Berisio R, Corti N, Pfister P, Yonath A, Böttger EC
* 23S rRNA 2058A→G alteration mediates ketolide resistance in combination with deletion in L22 (400 views)
Antimicrob Agents Ch (ISSN: 0066-4804, 1098-6596), 2006 Nov; 50(11): 3816-3823.
Impact Factor: 4.153
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Amit M, Berisio R, Baram D, Harms J, Bashan A, Yonath A
* A crevice adjoining the ribosome tunnel: Hints for cotranslational folding (387 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2005 Jun 13; 579(15): 3207-3213.
Impact Factor: 3.415
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Berisio R, Harms J, Schluenzen F, Zarivach R, Hansen HAS, Fucini P, Yonath A
* Structural insight into the antibiotic action of telithromycin against resistant mutants (418 views)
J Bacteriol Journal Of Bacteriology (ISSN: 0021-9193, 1098-5530), 2003 Jul; 185(14): 4276-4279.
Impact Factor: 4.175
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Berisio R, Schluenzen F, Harms J, Bashan A, Auerbach T, Baram D, Yonath A
* Structural insight into the role of the ribosomal tunnel in cellular regulation (375 views)
Nat Struct Biol (ISSN: 1072-8368), 2003 May; 10(5): 366-370.
Impact Factor: 11.579
View Export to BibTeX Export to EndNote
Bashan A, Agmon I, Zarivach R, Schluenzen F, Harms J, Berisio R, Bartels H, Franceschi F, Auerbach T, Hansen HAS, Kossoy E, Kessler M, Yonath A
* Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression (461 views)
Mol Cell (ISSN: 1097-2765, 1097-4164), 2003 Jan; 11(1): 91-102.
Impact Factor: 16.835
View Export to BibTeX Export to EndNote
11 Records (11 excluding Abstracts).
Total impact factor: 59.701 (59.701 excluding Abstracts).
Total 5 year impact factor: 53.239 (53.239 excluding Abstracts).
Total impact factor: 59.701 (59.701 excluding Abstracts).
Total 5 year impact factor: 53.239 (53.239 excluding Abstracts).
340 views. Last view on Thursday 02 March 2023, 3:52:22
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