𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Observation ofEscherichia coliRibosomal Proteins and Their Posttranslational Modifications by Mass Spectrometry

✍ Scribed by Randy J. Arnold; James P. Reilly

Book ID
102566260
Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
108 KB
Volume
269
Category
Article
ISSN
0003-2697

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✦ Synopsis

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 Nterminal 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.

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## Abstract Histones typically play a role in DNA packaging and transcription regulation. These proteins are heavily modified by acetylation, methylation, phosphorylation and/or ubiquitination, and various combinations of these modifications alter histone functions and form the basis of the histone