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Expanding the genetic code of Escherichia coli with phosphoserine.

O-phosphoserine (Sep), the most abundant phosphoamino acid, is not genetically encoded but synthesized posttranslationally by a complex network of kinases and phosphatases. Park et al. (p. 1151) engineered an Escherichia coli strain that was able to incorporate Sep directly into proteins. The strain... Full description

Journal Title: Science (New York N.Y.), August 26, 2011, Vol.333(6046), pp.1151-1154
Main Author: Park, Hee-Sung
Other Authors: Hohn, Michael J , Umehara, Takuya , Guo, Li-Tao , Osborne, Edith M , Benner, Jack , Noren, Christopher J , Rinehart, Jesse , Söll, Dieter
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1095-9203 ; DOI: 10.1126/science.1207203
Link: http://search.proquest.com/docview/885560941/?pq-origsite=primo
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recordid: proquest885560941
title: Expanding the genetic code of Escherichia coli with phosphoserine.
format: Article
creator:
  • Park, Hee-Sung
  • Hohn, Michael J
  • Umehara, Takuya
  • Guo, Li-Tao
  • Osborne, Edith M
  • Benner, Jack
  • Noren, Christopher J
  • Rinehart, Jesse
  • Söll, Dieter
subjects:
  • Amino Acyl-Trna Synthetases–Metabolism
  • Anticodon–Pharmacology
  • Chloramphenicol–Genetics
  • Chloramphenicol O-Acetyltransferase–Drug Effects
  • Codon, Terminator–Genetics
  • Drug Resistance, Bacterial–Metabolism
  • Escherichia Coli–Biosynthesis
  • Genetic Code–Chemistry
  • Genetic Engineering–Genetics
  • Humans–Metabolism
  • MAP Kinase Kinase 1–Genetics
  • Peptide Elongation Factor Tu–Metabolism
  • Phosphoserine–Genetics
  • Protein Engineering–Metabolism
  • Protein Modification, Translational–Metabolism
  • RNA, Bacterial–Genetics
  • RNA, Transfer, Amino Acid-Specific–Biosynthesis
  • RNA, Transfer, Amino Acyl–Biosynthesis
  • RNA, Transfer, Cys–Biosynthesis
  • Recombinant Fusion Proteins–Biosynthesis
  • Transfer RNA Aminoacylation–Biosynthesis
  • Anticodon
  • Codon, Terminator
  • RNA, Bacterial
  • RNA, Transfer, Amino Acid-Specific
  • RNA, Transfer, Amino Acyl
  • RNA, Transfer, Cys
  • Recombinant Fusion Proteins
  • Phosphoserine
  • Chloramphenicol
  • Chloramphenicol O-Acetyltransferase
  • MAP Kinase Kinase 1
  • Map2k1 Protein, Human
  • Peptide Elongation Factor Tu
  • Amino Acyl-Trna Synthetases
ispartof: Science (New York, N.Y.), August 26, 2011, Vol.333(6046), pp.1151-1154
description: O-phosphoserine (Sep), the most abundant phosphoamino acid, is not genetically encoded but synthesized posttranslationally by a complex network of kinases and phosphatases. Park et al. (p. 1151) engineered an Escherichia coli strain that was able to incorporate Sep directly into proteins. The strain harbors a Sep-accepting transfer RNA (tRNASep), its cognate Sep-tRNA synthetase, and an elongation factor-Tu engineered to permit Sep-tRNASep binding. The system was used to synthesize a human kinase with one or two Sep residues inserted at specific sites. The ability to biosynthesize specific phosphoproteins directly will be very helpful for detailed studies of their enzyme and substrate properties. O-Phosphoserine (Sep), the most abundant phosphoamino acid in the eukaryotic phosphoproteome, is not encoded in the genetic code, but synthesized posttranslationally. Here, we present an engineered system for specific cotranslational Sep incorporation (directed by UAG) into any desired position...
language: eng
source:
identifier: E-ISSN: 1095-9203 ; DOI: 10.1126/science.1207203
fulltext: no_fulltext
issn:
  • 10959203
  • 1095-9203
url: Link


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titleExpanding the genetic code of Escherichia coli with phosphoserine.
creatorPark, Hee-Sung ; Hohn, Michael J ; Umehara, Takuya ; Guo, Li-Tao ; Osborne, Edith M ; Benner, Jack ; Noren, Christopher J ; Rinehart, Jesse ; Söll, Dieter
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identifierE-ISSN: 1095-9203 ; DOI: 10.1126/science.1207203
subjectAmino Acyl-Trna Synthetases–Metabolism ; Anticodon–Pharmacology ; Chloramphenicol–Genetics ; Chloramphenicol O-Acetyltransferase–Drug Effects ; Codon, Terminator–Genetics ; Drug Resistance, Bacterial–Metabolism ; Escherichia Coli–Biosynthesis ; Genetic Code–Chemistry ; Genetic Engineering–Genetics ; Humans–Metabolism ; MAP Kinase Kinase 1–Genetics ; Peptide Elongation Factor Tu–Metabolism ; Phosphoserine–Genetics ; Protein Engineering–Metabolism ; Protein Modification, Translational–Metabolism ; RNA, Bacterial–Genetics ; RNA, Transfer, Amino Acid-Specific–Biosynthesis ; RNA, Transfer, Amino Acyl–Biosynthesis ; RNA, Transfer, Cys–Biosynthesis ; Recombinant Fusion Proteins–Biosynthesis ; Transfer RNA Aminoacylation–Biosynthesis ; Anticodon ; Codon, Terminator ; RNA, Bacterial ; RNA, Transfer, Amino Acid-Specific ; RNA, Transfer, Amino Acyl ; RNA, Transfer, Cys ; Recombinant Fusion Proteins ; Phosphoserine ; Chloramphenicol ; Chloramphenicol O-Acetyltransferase ; MAP Kinase Kinase 1 ; Map2k1 Protein, Human ; Peptide Elongation Factor Tu ; Amino Acyl-Trna Synthetases
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descriptionO-phosphoserine (Sep), the most abundant phosphoamino acid, is not genetically encoded but synthesized posttranslationally by a complex network of kinases and phosphatases. Park et al. (p. 1151) engineered an Escherichia coli strain that was able to incorporate Sep directly into proteins. The strain harbors a Sep-accepting transfer RNA (tRNASep), its cognate Sep-tRNA synthetase, and an elongation factor-Tu engineered to permit Sep-tRNASep binding. The system was used to synthesize a human kinase with one or two Sep residues inserted at specific sites. The ability to biosynthesize specific phosphoproteins directly will be very helpful for detailed studies of their enzyme and substrate properties. O-Phosphoserine (Sep), the most abundant phosphoamino acid in the eukaryotic phosphoproteome, is not encoded in the genetic code, but synthesized posttranslationally. Here, we present an engineered system for specific cotranslational Sep incorporation (directed by UAG) into any desired position...
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titleExpanding the genetic code of Escherichia coli with phosphoserine.
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