Mar 27, 1999

Key role of barstar Cys-40 residue in the mechanism of heat denaturation of bacterial ribonuclease complexes with barstar

FEBS Letters
I I ProtasevichA A Makarov

Abstract

The mechanism by which barnase and binase are stabilized in their complexes with barstar and the role of the Cys-40 residue of barstar in that stabilization have been investigated by scanning microcalorimetry. Melting of ribonuclease complexes with barstar and its Cys-82-Ala mutant is described by two 2-state transitions. The lower-temperature one corresponds to barstar denaturation and the higher-temperature transition to ribonuclease melting. The barstar mutation Cys-40-Ala, which is within the principal barnase-binding region of barstar, simplifies the melting to a single 2-state transition. The presence of residue Cys-40 in barstar results in additional stabilization of ribonuclease in the complex.

Mentioned in this Paper

Bacillus intermedius ribonuclease
Bacterial Proteins
Complex (molecular entity)
Mutagenesis, Site-Directed
Plain X-ray
Sulfur
Abufne
Bacillus amyloliquefaciens ribonuclease
Alkaline Ribonuclease
Cysteine

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