Expanded cellular amino acid pools containing phosphoserine, phosphothreonine, and phosphotyrosine.

ABSTRACT: Adding nonstandard amino acids to the genetic code of E. coli expands the chemical and biological functional space for proteins. This is accomplished with engineered, orthogonal aminoacyl-tRNA synthetase and tRNA pairs that require a nonstandard amino acid in sufficient intracellular quantities to support protein synthesis. While cotranslational insertion of phosphoserine into proteins has been accomplished, conditions that modulate intracellular phosphoamino acid concentrations are still poorly understood. Here we used genetic and metabolic engineering to increase the free intracellular levels of phosphoserine in E. coli. We show that deletion of the phosphoserine phosphatase serB elevates the intracellular levels of phosphoserine within ranges comparable to those of standard amino acids.

SUBMITTER: Steinfeld JB 

PROVIDER: S-EPMC4027946 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature