Publication | Closed Access
Methionine-Selenomethionine Parallels in E. coli Polypeptide Chain Initiation and Synthesis
17
Citations
0
References
1972
Year
Se MetBiosynthesisEngineeringProtein ExpressionBiochemistryNatural SciencesProtein BiosynthesisMolecular BiologySynthetic BiologyPeptide SynthesisF2 Viral RnaProtein EngineeringStructure-function Enzyme KineticsMolecular MicrobiologyGene ExpressionMethionine-selenomethionine ParallelsProtein Synthesis
Using a cell-free synthesizing system and natural messenger (f2 viral RNA), we observed that selenomethionyl-tRNA participated in polypeptide synthesis to about the same extent as methionyl-tRNA. Studies on the role of Se Met in the initiation of protein synthesis indicated that N-formyl Se Met-tRNA can function as an initiator of protein synthesis as it has been established for N-formyl Met-tRNA. It is concluded that in E. coli Se Met is incorporated into polypeptides via the Met pathway, including the initiation mechanism involving the N-formylated aminoacyl-tRNA.