| Chapter title |
Reconstitution of the Arginyltransferase (ATE1) Iron-Sulfur Cluster.
|
|---|---|
| Chapter number | 23 |
| Book title |
Protein Arginylation
|
| Published in |
Methods in molecular biology, January 2023
|
| DOI | 10.1007/978-1-0716-2942-0_23 |
| Pubmed ID | |
| Book ISBNs |
978-1-07-162941-3, 978-1-07-162942-0
|
| Authors |
Van, Verna, Smith, Aaron T, Smith, Aaron T. |
| Abstract |
As global regulators of eukaryotic homeostasis, arginyltransferases (ATE1s) have essential functions within the cell. Thus, the regulation of ATE1 is paramount. It was previously postulated that ATE1 was a hemoprotein and that heme was an operative cofactor responsible for enzymatic regulation and inactivation. However, we have recently shown that ATE1 instead binds an iron-sulfur ([Fe-S]) cluster that appears to function as an oxygen sensor to regulate ATE1 activity. As this cofactor is oxygen-sensitive, purification of ATE1 in the presence of O2 results in cluster decomposition and loss. Here, we describe an anoxic chemical reconstitution protocol to assemble the [Fe-S] cluster cofactor in Saccharomyces cerevisiae ATE1 (ScATE1) and Mus musculus ATE1 isoform 1 (MmATE1-1). |
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