Beta-methylthio-aspartic acid: identification of a novel posttranslational modification in ribosomal protein S12 from Escherichia coli.
Utilizing microscale chemical derivatization reactions and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, we have identified a novel posttranslational modification of aspartic acid, beta-methylthio-aspartic acid. The modified residue is located at position 88 in ribosomal protein S12 from Escherichia coli, a phylogenetically conserved protein that has been implicated in maintaining translational accuracy of the ribosome.
Kowalak
J A
JA
Department of Biochemistry, University of Washington, Seattle 98195, USA.
Walsh
K A
KA
D001224:Aspartic Acid / Q000737:chemistry* / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D004926:Escherichia coli / Q000737:chemistry*; D006868:Hydrolysis; D010084:Oxidation-Reduction; D010446:Peptide Fragments / Q000032:analysis / Q000737:chemistry; D011499:Protein Processing, Post-Translational; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D014357:Trypsin / Q000378:metabolism
D010446:Peptide Fragments; D012269:Ribosomal Proteins; C034212:ribosomal protein S12; D001224:Aspartic Acid; D014357:Trypsin