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Inside Cover: Genetic Code Expansion by Degeneracy Reprogramming of Arginyl Codons (ChemBioChem 13/2016)
Author(s) -
Lee Ki Baek,
Hou Chen Yuan,
Kim ChaeEun,
Kim DongMyung,
Suga Hiroaki,
Kang Taek Jin
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600326
Subject(s) - degeneracy (biology) , genetic code , stop codon , reprogramming , biology , genetics , cover (algebra) , reading frame , amino acid , gene , codon usage bias , computational biology , open reading frame , genome , peptide sequence , engineering , mechanical engineering
The inside cover picture shows a schematic idea of the concept of degeneracy reprogramming. Mutating a given protein with non‐proteinogenic amino acid (NAA) has become an invaluable tool in protein engineering. Incorporating a NAA is usually accomplished by reprogramming one of the stop codons, so frequently, multiple NAAs cannot be used at the same time because of the lack of usable codons other than the stop codon. In the universal genetic code system, arginine takes six codons out of 64 possible combinations (six rooms in the Hotel Universal are occupied by Arg). Conceptually, one could free up five codons to use for encoding NAAs by assigning only one codon to arginine (two rooms in the Repro Hotel are occupied by NAA and Arg, but there are still four rooms left empty). We have taken advantage of 1) the specific tRNase activity of colicin D toward arginyl tRNAs, and 2) the open nature of a cell‐free protein synthesis system to prove the concept that they call degeneracy reprogramming. More information can be found in the communication by T. J. Kang et al. on page 1198 in Issue 13, 2016 (DOI: 10.1002/cbic.201600111).