Synthesis of a novel histidine analogue and its efficient incorporation into a protein in vivo.
Proteins containing unnatural amino acids have immense potential in biotechnology and medicine. We prepared several histidine analogues including a novel histidine analogue, beta-(1,2,3-triazol-4-yl)-DL-alanine. These histidine analogues were assayed for translational activity in histidine-auxotrophic Escherichia coli strain UTH780. We observed that several histidine analogues, including our novel histidine analogue, were efficiently incorporated into the protein in vivo; however, other analogues were rejected. These results suggest that the hydrogen atom at a specific position seriously affects incorporation.
Ikeda
Yutaka
Y
Department of Chemistry and Biotechnology, School of Engineering, University of Tokyo, 7-3-1 Hongo, Tokyo 113-8656, Japan.
Kawahara
Shun-ichi
S
Taki
Masumi
M
Kuno
Atsushi
A
Hasegawa
Tsunemi
T
Taira
Kazunari
K
D001426:Bacterial Proteins / Q000096:biosynthesis*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000737:chemistry; D006639:Histidine / Q000031:analogs & derivatives / Q000138:chemical synthesis* / Q000737:chemistry*; D008958:Models, Molecular; D018716:Molecular Mimicry; D009154:Mutation
D001426:Bacterial Proteins; C487883:beta-(1,2,3-triazol-4-yl)-DL-alanine; D006639:Histidine