Abstract
A self-cleaving element for use in bioseparations has been derived from a naturally occurring, 43 kDa protein splicing element (intein) through a combination of protein engineering and random mutagenesis. A mini-intein (18 kDa) previously engineered for reduced size had compromised activity and was therefore subjected to random mutagenesis and genetic selection. In one selection a mini-intein was isolated with restored splicing activity, while in another, a mutant was isolated with enhanced, pH-sensitive C-terminal cleavage activity. The enhanced-cleavage mutant has utility in affinity fusion-based protein purification. These mutants also provide new insights into the structural and functional roles of some conserved residues in protein splicing.
| Original language | English |
|---|---|
| Pages (from-to) | 889-892 |
| Number of pages | 4 |
| Journal | Nature Biotechnology |
| Volume | 17 |
| Issue number | 9 |
| DOIs | |
| State | Published - Sep 1999 |
Keywords
- Function of conserved residues
- Mini-intein mutants
- PH-sensitive cleavage
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