TAILIEUCHUNG - Báo cáo khoa học: Pyrimidine-specific ribonucleoside hydrolase from the archaeon Sulfolobus solfataricus – biochemical characterization and homology modeling

We report the characterization of the pyrimidine-specific ribonucleoside hydrolase from the hyperthermophilic archaeon Sulfolobus solfataricus (SsCU-NH). The gene SSO0505 encoding SsCU-NH was cloned and expressed in Escherichia coliand the recombinant protein was purified to homogeneity. | ễFEBS Journal Pyrimidine-specific ribonucleoside hydrolase from the archaeon Sulfolobus solfataricus - biochemical characterization and homology modeling Marina Porcelli1 2 Luigi Concilio1 lolanda Peluso1 Anna Marabotti3 Angelo Facchiano3 and Giovanna Cacciapuoti1 1 Dipartimento di Biochimica e Biofisica F. Cedrangolo Seconda Universita di Napoli Italy 2 Consorzio Interuniversitario Biostrutture e Biosistemi INBB Rome Italy 3 Istituto di Scienze dell Alimentazione delCNR Avellino Italy Keywords homology modeling hyperthermostability nucleoside hydrolase nucleoside metabolism Sulfolobus solfataricus Correspondence M. Porcelli Dipartimento di Biochimica e Biofisica F. Cedrangolo Seconda University di Napoli Via Costantinopoli 16 Napoli 80138 Italy Fax 39 081 5667519 Tel 39 081 5667545 E-mail Received 23 November 2007 revised 11 February 2008 accepted 20 February 2008 doi We report the characterization of the pyrimidine-specific ribonucleoside hydrolase from the hyperthermophilic archaeon Sulfolobus solfataricus SsCU-NH . The gene SSO0505 encoding SsCU-NH was cloned and expressed in Escherichia coli and the recombinant protein was purified to homogeneity. SsCU-NH is a homotetramer of 140 kDa that recognizes uridine and cytidine as substrates. SsCU-NH shares 34 sequence identity with pyrimidine-specific nucleoside hydrolase from E. coli YeiK. The alignment of the amino acid sequences of SsCU-NH with nucleoside hydrolases whose 3D structures have been solved indicates that the amino acid residues involved in the calcium- and ribose-binding sites are preserved. SsCU-NH is highly thermophilic with an optimum temperature of 100 C and is characterized by extreme thermodynamic stability Tm 106 C and kinetic stability 100 residual activity after 1 h incubation at 90 C . Limited proteolysis indicated that the only proteolytic cleavage site is localized in the C-terminal region and that the C-terminal peptide is .

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