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Ansgar Siemer, Manuel Masip, Nelson Carreras, Lucía García-Ortega, Mercedes Oñaderra, Marta Bruix, Álvaro Martínez del Pozo, José G. Gavilanes

Conserved asparagine residue 54 of ?-sarcin plays a role in protein stability and enzyme activity

Keywords: ?-sarcin, protein stability, ribonuclease, RNase T1

Asparagine 54 of ?-sarcin is a conserved residue within the proteins of the ribotoxin family of microbial ribonucleases. It is located in loop 2 of the protein, which lacks repetitive secondary structure elements but exhibits a well-defined conformation. Five mutant variants at this residue have been produced and characterized. The spectroscopic characterization of these proteins indicates that the overall conformation is not changed upon mutation. Activity and denaturation assays show that Asn-54 largely contributes to protein stability, and its presence is a requirement for the highly specific inhibitory activity of these ribotoxins on ribosomes.

Biological Chemistry, Walter de Gruyter

Print ISSN: 1431-6730
Volume: 385, 12/2004
Pages: 1165 - 1170

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