Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1951364 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2008 | 7 Pages |
Abstract
Determination of the substrate specificity of site-specific proteases helps define their physiological roles. We developed a yeast-based system for defining the minimal substrate specificity of site-specific proteases, within the context of a protein. Using this system, we characterized the P4–P1 substrate specificity of the nematode apoptotic caspase CED-3. Apart from an absolute requirement for aspartate at the P1 position, CED-3 is a relatively promiscuous caspase capable of cleaving substrates bearing many amino acids at P4–P2 sites.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Sarah J. Westein, Fiona L. Scott, Christine J. Hawkins,