RESUMO
This review describes the use of a simple genetic system that has provided important insight into the process of folding and, of its flipside, that of protein aggregation. These studies make use of the tail protein of the bacterial virus P22 which infects Salmonella typhimurium. This folding system serves as a model for a number protein structural elements and may also provide important insights into disease-related protein folding defects at a time when an increasing number of diseases are being shown to be due to protein folding alterations
Assuntos
Humanos , /genética , Técnicas In Vitro , Dobramento de Proteína , Proteínas da Cauda Viral/genética , Aminoácidos/genética , Aminoácidos/metabolismo , /fisiologia , DNA Viral/genética , Hidrólise , Mutação , Conformação Proteica , Salmonella typhimurium/virologiaRESUMO
The present study demonstrates the presence of considerable levels of 2',5'-oligoA synthetase activity in tissue extracts from mice. The interferon inducer, poly(I).poly(C), induced the synthetase activity in all the tissue extracts in vivo. Similarly, a significant amount of endonuclease RNase F activity is found to be present in these tissue extracts. But interferon induction does not seem to have any significant effect on RNase F activity.