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

Abstract:

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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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2008.04.067

Authors


Journal:
Journal of molecular biology
Volume:
380
Issue:
2
Pages:
404-414
Publication date:
2008-07-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:395def44-2d75-4b17-9f64-6ef5a4c4f483
Source identifiers:
59312
Local pid:
pubs:59312

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