| Chapter title |
Selenocysteine-Mediated Expressed Protein Ligation of SELENOM
|
|---|---|
| Chapter number | 19 |
| Book title |
Selenoproteins
|
| Published in |
Methods in molecular biology, January 2018
|
| DOI | 10.1007/978-1-4939-7258-6_19 |
| Pubmed ID | |
| Book ISBNs |
978-1-4939-7257-9, 978-1-4939-7258-6
|
| Authors |
Jun Liu, Qingqing Chen, Sharon Rozovsky, Liu, Jun, Chen, Qingqing, Rozovsky, Sharon |
| Abstract |
A sizeable fraction of the selenoproteome encodes oxidoreductases possessing a thioredoxin fold, a structural motif that is shared among a diverse group of enzymes. In these oxidoreductases, the active site is comprised of a cysteine and a selenocysteine separated by one to two amino acids. In a subset of these selenoproteins, such as human SELENOH, SELENOM, SELENOT, SELENOV, SELENOW, and SELENOF, this redox motif is positioned immediately after the first β-sheet in a short loop, and is essential for interactions with its substrate or partners. Here, we describe the preparation of a representative member of this group, SELENOM, by selenocysteine-driven expressed protein ligation. The preparation employs a peptide bond formation between two protein fragments expressed recombinantly in E. coli. This method can be employed to prepare other selenoproteins. |
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