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

  • Ansgar Siemer , Manuel Masip , Nelson Carreras , Lucía García-Ortega , Mercedes Oñaderra , Marta Bruix , Álvaro Martínez del Pozo and José G. Gavilanes
Published/Copyright: June 1, 2005
Biological Chemistry
From the journal Volume 385 Issue 12

Abstract

Asparagine 54 of α-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.

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Published Online: 2005-06-01
Published in Print: 2004-12-01

©2004 by Walter de Gruyter Berlin New York

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