TAILIEUCHUNG - Báo cáo khoa học: Purine nucleoside phosphorylases from hyperthermophilic Archaea require a CXC motif for stability and folding

5¢-Deoxy-5¢-methylthioadenosine phosphorylase II fromSulfolobus solfatari-cus (SsMTAPII) and purine nucleoside phosphorylase from Pyrococcus furiosus (PfPNP) are hyperthermophilic purine nucleoside phosphorylases stabilized by intrasubunit disulfide bonds. In their C-terminus, both enzymes harbour a CXC motif analogous to the CXXC motif present at the active site of eukaryotic protein disulfide isomerase. | ỊFEBS Journal Purine nucleoside phosphorylases from hyperthermophilic Archaea require a CXC motif for stability and folding Giovanna Cacciapuoti lolanda Peluso Francesca Fuccio and Marina Porcelli Department of Biochemistry and Biophysics F. Cedrangolo Second University of Naples Italy Keywords 5 -deoxy-5 -methylthioadenosine phosphorylase CXC motif and oxidative protein folding disulfide bonds hyperthermophilic proteins purine nucleoside phosphorylase Correspondence G. Cacciapuoti Dipartimento di Biochimica e Biofisica F. Cedrangolo Seconda Universita di Napoli Via Costantinopoli 16 80138 Napoli Italy Fax 39 081 5667519 Tel 39 081 5667519 E-mail Received 5 June 2009 revised 22 July 2009 accepted 29 July 2009 doi 5 -Deoxy-5 -methylthioadenosine phosphorylase II from Sulfolobus solfatari-cus SsMTAPII and purine nucleoside phosphorylase from Pyrococcus furiosus PfPNP are hyperthermophilic purine nucleoside phosphorylases stabilized by intrasubunit disulfide bonds. In their C-terminus both enzymes harbour a CXC motif analogous to the CXXC motif present at the active site of eukaryotic protein disulfide isomerase. By monitoring the refolding of SsMTAPII PfPNP and their mutants lacking the C-terminal cysteine pair after guanidine-induced unfolding we demonstrated that the CXC motif is required for the folding of these enzymes. Moreover two synthesized CXC-containing peptides with the same amino acid sequences present in the C-terminal regions of SsMTAPII and PfPNP were found to act as in vitro catalysts of oxidative folding. These small peptides are involved in the folding of partially refolded SsMTAPII PfPNP and their CXC-lacking mutants with a concomitant recovery of their catalytic activity thus indicating that the CXC motif is necessary to obtain complete reversibility from the unfolded state of the two proteins. The two CXC-containing peptides are also able to reactivate scrambled RNaseA. The data .

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