Site-specific cleavage of a protein via introducing a hydroxy acid derivative in the main chain by using four-base
1Department of Bioscience and Biotechnology, Okayama University, 3-1-1 Tsushi Manaka, Okayama 700, Japan.
Abstract:
Site-specific incorporation of the tyrosine isostere (2-Hydroxy-3-(4-hydroxy-phenyl)-propionic acid) into streptavidin was accomplished by in vitro frameshift suppression of a CGGG 4-base mutation with a chemically acylated frameshift suppressor tRNA(cccg). The mutant, in which the backbone amide linkage is replaced by an ester linkage, is hydrolyzed under neutral condition. The cleavage rate of the protein backbone at a single-predetermined site was strongly depended on the incorporated position of the isostere.
More Related Videos
08:34OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
Published on: February 5, 2020
13:53Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes
Published on: December 19, 2020
Related Concept Videos
From DNA to Protein
Conservative Site-specific Recombination and Phase Variation
The recognition sites for Cre recombinase called LoxP...
tRNA Activation
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Leaky Scanning
The Proteasome
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
