Stability of mutant actins
- 15 February 1991
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 274 (1), 301-303
- https://doi.org/10.1042/bj2740301
Abstract
Mutants of the Drosophila Act88F actin gene were transcribed and translated in vitro and their relative stabilities were examined using urea gradient gel electrophoresis. Most of the mutant actins (E334K, E364K, G366D, G368E and R372H) were as stable as the wild-type. V339I had a slight decrease in stability, and E316K was the least stable. The causes of the differences are discussed and contrasted with the behaviour of the mutants in vivo, where E316K has normal stability and V339I is the least stable.Keywords
This publication has 20 references indexed in Scilit:
- Alteration in crossbridge kinetics caused by mutations in actinNature, 1990
- Gel electrophoresis in studies of protein conformation and foldingAnalytical Biochemistry, 1984
- Synthesis and Turnover of Cytoskeletal Proteins in Cultured AstrocytesJournal of Neurochemistry, 1984
- Turnover of excess hemoglobin alpha chains in beta-thalassemic cells is ATP-dependent.Journal of Biological Chemistry, 1983
- [18] Purification of muscle actinMethods in Enzymology, 1982
- Kinetic study of protein unfolding and refolding using urea gradient electrophoresisJournal of Molecular Biology, 1980
- Electrophoretic analysis of the unfolding of proteins by ureaJournal of Molecular Biology, 1979
- Is protein turnover thermodynamically controlled?Journal of Biological Chemistry, 1978
- Intracellular Protein Degradation in Mammalian and Bacterial Cells: Part 2Annual Review of Biochemistry, 1976
- Intracellular Protein Degradation in Mammalian and Bacterial CellsAnnual Review of Biochemistry, 1974