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A Postproteomic Approach to Study Ribosome Assembly
Author(s) -
Williamson James R.
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a45-d
Subject(s) - ribosome , 30s , ribosomal rna , ribosomal protein , protein subunit , eukaryotic small ribosomal subunit , eukaryotic large ribosomal subunit , mass spectrometry , chemistry , computational biology , biochemistry , biology , chromatography , 18s ribosomal rna , rna , gene
Assembly of the 30S ribosomal subunit from purified components takes place spontaneously in vitro. The basic pathway for assembly was worked out by Nomura and colleagues over 30 years ago, and the Nomura assembly map describes the thermodynamic assembly pathway for the 30S subunit. We have recently developed an isotope pulse‐chase assay to monitor the binding of the 20 ribosomal subunits to 16S rRNA in real time. Our first experiments to measure assembly kinetics were carried out using MALDI‐TOF mass spectrometry to measure the isotopomer ratio of intact ribosomal proteins. We have extended this method to make use of proteomic mass spectrometry methods. New results from the isotope pulse‐chase assay will be presented using subsets of ribosomal proteins in an effort to further understand the assembly landscape of the 30S subunit.