Site-specific cleavage of a protein via introducing a hydroxy acid derivative in the main chain by using four-base codon/anticodon pairs.
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.
Taki
M
M
Department of Bioscience and Biotechnology, Okayama University, 3-1-1 Tsushi Manaka, Okayama 700, Japan.
Hohsaka
T
T
Sisido
M
M
D000926:Anticodon / Q000737:chemistry*; D003062:Codon / Q000737:chemistry*; D010666:Phenylpropionates / Q000737:chemistry*; D014176:Protein Biosynthesis; D019809:Streptavidin / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D014443:Tyrosine / Q000737:chemistry
C476362:2-hydroxy-3-(4-hydroxyphenyl)propionic acid; D000926:Anticodon; D003062:Codon; D010666:Phenylpropionates; D014443:Tyrosine; D019809:Streptavidin