Acetylation of L12 increases interactions in the Escherichia coli ribosomal stalk complex.

Journal article

The ribosomal stalk complex in Escherichia coli consists of L10 and four copies of L7/L12, and is largely responsible for binding and recruiting translation factors. Structural characterisation of this stalk complex is difficult, primarily due to its dynamics. Here, we apply mass spectrometry to follow post-translational modifications and their effect on structural changes of the stalk proteins on intact ribosomes. Our results show that increased acetylation of L12 occurs during the stationar...

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Authors: Gordiyenko, Y; Deroo, S; Zhou, M; Videler, H; Robinson, C

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 380
• Issue: 2
• Pages: 404-414
• Publication date: 2008-07-01
• DOI: 10.1016/j.jmb.2008.04.067
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Escherichia coli; Models, Molecular; Molecular Weight; Ribosomal Proteins; Ribosomes; Molecular Sequence Data; Protein Subunits; Mass Spectrometry; Protein Processing, Post-Translational; Protein Structure, Quaternary; Escherichia coli Proteins; Acetylation