Chapter title |
Assaying ATE1 Activity in Yeast by β-Gal Degradation.
|
---|---|
Chapter number | 8 |
Book title |
Protein Arginylation
|
Published in |
Methods in molecular biology, January 2015
|
DOI | 10.1007/978-1-4939-2935-1_8 |
Pubmed ID | |
Book ISBNs |
978-1-4939-2934-4, 978-1-4939-2935-1
|
Authors |
Kashina, Anna S, Anna S. Kashina |
Editors |
Anna S. Kashina |
Abstract |
In 1980s it was found that addition of N-terminal Arg to proteins induces their ubiquitination and degradation by the N-end rule pathway. While this mechanism applies only to the proteins which also have other features of the N-degron (including a closely adjacent Lys that is accessible for ubiquitination), several test substrates have been found to follow this mechanism very efficiently after ATE1-dependent arginylation. Such property enabled researchers to test ATE1 activity in cells indirectly by assaying for the degradation of such arginylation-dependent substrates. The most commonly used substrate for this assay is E. coli beta galactosidase (beta-Gal) because its activity can be easily measured using standardized colorimetric assays. Here we describe this method, which has served as a quick and easy way to characterize ATE1 activity during identification of arginyltransferases in different species. |
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