2022
Enhanced access to the human phosphoproteome with genetically encoded phosphothreonine
Moen J, Mohler K, Rogulina S, Shi X, Shen H, Rinehart J. Enhanced access to the human phosphoproteome with genetically encoded phosphothreonine. Nature Communications 2022, 13: 7226. PMID: 36433969, PMCID: PMC9700786, DOI: 10.1038/s41467-022-34980-5.Peer-Reviewed Original ResearchConceptsUbiquitous post-translational modificationCo-translational insertionKinase activation mechanismProtein interaction platformOrthogonal translation systemProtein-protein interactionsPost-translational modificationsPhospho-amino acidsAminoacyl-tRNA synthetaseHuman phosphoproteomePhosphorylation eventsTRNA pairsFunctional assignmentCellular processesProtein phosphorylationUpstream kinasePhysiological functionsActivation mechanismTranslation systemKinasePhosphorylationInteraction platformPhosphoproteomePhosphothreoninePhospho
2014
Expanded Cellular Amino Acid Pools Containing Phosphoserine, Phosphothreonine, and Phosphotyrosine
Steinfeld JB, Aerni HR, Rogulina S, Liu Y, Rinehart J. Expanded Cellular Amino Acid Pools Containing Phosphoserine, Phosphothreonine, and Phosphotyrosine. ACS Chemical Biology 2014, 9: 1104-1112. PMID: 24646179, PMCID: PMC4027946, DOI: 10.1021/cb5000532.Peer-Reviewed Original ResearchConceptsNonstandard amino acidsAmino acidsGenetic codeOrthogonal aminoacyl-tRNA synthetaseCellular amino acid poolsIntracellular levelsPhosphorylated amino acidsAminoacyl-tRNA synthetaseE. coliLow-phosphate mediumAmino acid poolCotranslational insertionTRNA pairsMetabolic engineeringRecombinant proteinsDeficient cellsStandard amino acidsProtein synthesisWT cellsPhosphoserinePhosphotyrosinePhosphothreonineProteinAcid poolColi
2012
Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion
Heinemann IU, Rovner AJ, Aerni HR, Rogulina S, Cheng L, Olds W, Fischer JT, Söll D, Isaacs FJ, Rinehart J. Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion. FEBS Letters 2012, 586: 3716-3722. PMID: 22982858, PMCID: PMC3473164, DOI: 10.1016/j.febslet.2012.08.031.Peer-Reviewed Original ResearchConceptsUAG codonEscherichia coli protein synthesisRelease factor 1Aminoacyl-tRNA synthetaseCellular fitnessCodon reassignmentEssential genesElongation factorPhosphoserine phosphataseProtein synthesisRF-1Protein yieldTranslation systemFactor 1CodonAccompanying lossGFPUAAGenesSynthetaseDeletionWNK4FitnessPhosphataseExpression