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1. Two-dimensional IR correlation spectroscopy of mutants of the β-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus identifies the mechanism of quaternary structure stabilization and unravels the sequence of thermal unfolding events

Author

AUSILI, Alessio, primary, DI LAURO, Barbara, additional, COBUCCI-PONZANO, Beatrice, additional, BERTOLI, Enrico, additional, SCIRÈ, Andrea, additional, ROSSI, Mosè, additional, TANFANI, Fabio, additional, and MORACCI, Marco, additional

Published
2004
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2. Two-dimensional IR correlation spectroscopy of mutants of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus identifies the mechanism of quaternary structure stabilization and unravels the sequence of thermal unfolding events

Author

Barbara Di Lauro, Mosè Rossi, Fabio Tanfani, Alessio Ausili, Beatrice Cobucci-Ponzano, Enrico Bertoli, Marco Moracci, Andrea Scirè, Ausili, Alessio, DI LAURO, Barbara, Cobucci Ponzano, Beatrice, Bertoli, Enrico, Scirè, Andrea, Rossi, Mose', Tanfani, Fabio, and Moracci, Marco

Subjects
Models, Molecular, Protein Denaturation, Protein Folding, Hot Temperature, ved/biology.organism_classification_rank.species, quaternary structure, Biology, Arginine, Biochemistry, thermal stability, Protein Structure, Secondary, Protein structure, Sequence Analysis, Protein, Image Interpretation, Computer-Assisted, Spectroscopy, Fourier Transform Infrared, Histidine, protein structure, Protein Structure, Quaternary, Molecular Biology, Protein secondary structure, two-dimensional infrared spectroscopy, Thermostability, beta-glycosidase, Alanine, ved/biology, Sulfolobus solfataricus, Cell Biology, Recombinant Protein, Sulfolobus solfataricu, Recombinant Proteins, Crystallography, Amino Acid Substitution, Mutation, Protein folding, Protein quaternary structure, Glucosidase, Two-dimensional nuclear magnetic resonance spectroscopy, Glucosidases, Homotetramer, Research Article
Abstract

β-Glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus is a homotetramer with a higher number of ion pairs compared with mesophilic glycoside hydrolases. The ion pairs are arranged in large networks located mainly at the tetrameric interface of the molecule. In the present study, the structure and thermal stability of the wild-type β-glycosidase and of three mutants in residues R488 and H489 involved in the C-terminal ionic network were examined by FTIR (Fourier-transform IR) spectroscopy. The FTIR data revealed small differences in the secondary structure of the proteins and showed a lower thermostability of the mutant proteins with respect to the wild-type. Generalized 2D-IR (two-dimensional IR correlation spectroscopy) at different temperatures showed different sequences of thermal unfolding events in the mutants with respect to the wild-type, indicating that punctual mutations affect the unfolding and aggregation process of the protein. A detailed 2D-IR analysis of synchronous maps of the proteins allowed us to identify the temperatures at which the ionic network that stabilizes the quaternary structure of the native and mutant enzymes at the C-terminal breaks down. This evidence gives support to the current theories on the mechanism of ion-pair stabilization in proteins from hyperthermophilic organisms.

Published
2004
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3. Two-dimensional IR correlation spectroscopy of mutants of the beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus identifies the mechanism of quaternary structure stabilization and unravels the sequence of thermal unfolding events.

Author

Ausili A, Di Lauro B, Cobucci-Ponzano B, Bertoli E, Scirè A, Rossi M, Tanfani F, and Moracci M

Subjects
Alanine chemistry, Alanine genetics, Amino Acid Substitution genetics, Arginine chemistry, Arginine genetics, Glucosidases genetics, Histidine chemistry, Histidine genetics, Image Interpretation, Computer-Assisted methods, Models, Molecular, Protein Denaturation genetics, Protein Folding, Protein Structure, Quaternary genetics, Protein Structure, Secondary genetics, Recombinant Proteins chemistry, Recombinant Proteins genetics, Sequence Analysis, Protein methods, Sulfolobus solfataricus enzymology, Sulfolobus solfataricus genetics, Glucosidases chemistry, Hot Temperature, Mutation genetics, Spectroscopy, Fourier Transform Infrared methods
Abstract

Beta-glycosidase from the hyperthermophilic archaeon Sulfolobus solfataricus is a homotetramer with a higher number of ion pairs compared with mesophilic glycoside hydrolases. The ion pairs are arranged in large networks located mainly at the tetrameric interface of the molecule. In the present study, the structure and thermal stability of the wild-type beta-glycosidase and of three mutants in residues R488 and H489 involved in the C-terminal ionic network were examined by FTIR (Fourier-transform IR) spectroscopy. The FTIR data revealed small differences in the secondary structure of the proteins and showed a lower thermostability of the mutant proteins with respect to the wild-type. Generalized 2D-IR (two-dimensional IR correlation spectroscopy) at different temperatures showed different sequences of thermal unfolding events in the mutants with respect to the wild-type, indicating that punctual mutations affect the unfolding and aggregation process of the protein. A detailed 2D-IR analysis of synchronous maps of the proteins allowed us to identify the temperatures at which the ionic network that stabilizes the quaternary structure of the native and mutant enzymes at the C-terminal breaks down. This evidence gives support to the current theories on the mechanism of ion-pair stabilization in proteins from hyperthermophilic organisms.

Published
2004
Full Text
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