Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry.
Ribosomes from the K-12 strain of Escherichia coli were analyzed with good sensitivity and high mass accuracy using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Fifty-five of the 56 subunit proteins were observable. Mass spectral peak locations were consistent with previously reported post-translational modifications involving N-terminal methionine loss, methylation, thiomethylation, and acetylation for all but one case. The speed and accuracy of mass spectrometry make it a good candidate for phylogenetic studies of ribosomes and the observation of posttranslational modifications in other organisms.
Arnold
R J
RJ
Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
Reilly
J P
JP
D004926:Escherichia coli / Q000737:chemistry*; D013058:Mass Spectrometry / Q000379:methods*; D011499:Protein Processing, Post-Translational; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism; D012680:Sensitivity and Specificity
D012269:Ribosomal Proteins