Article
Overexpression of L-isoaspartate O-methyltransferase in Escherichia coli increases heat shock survival by a mechanism independent of methyltransferase activity.
The Journal of biological chemistry - 19 Dec 2003
Kindrachuk Jason, Parent Jennifer, Davies Gerald F, Dinsmore Michael, Attah-Poku Samuel, Napper Scott
Abstract excerpt
Over time and under stressing conditions proteins are susceptible to a variety of spontaneous covalent modifications. One of the more commonly occurring types of protein damage is deamidation; the conversion of asparagines into aspartyls and isoaspartyls. The physiological significance of isoaspartyl formation is emphasized by the presence of the conserved enzyme L-isoaspartyl O-methyltransferase (PIMT), whose...
Topics
- Amino Acid Sequence
- Escherichia coli
- Gene Expression Regulation
- HSP70 Heat-Shock Proteins
- Heat-Shock Response
- Kinetics
- Mutation
- Protein Binding
- Protein D-Aspartate-L-Isoaspartate Methyltransferase
- Sequence Alignment
- Transduction, Genetic