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  Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome.

Polikanov, Y. S., Osterman, I. A., Szal, T., Tashlitsky, V. N., Serebryakova, M. V., Kusochek, P., et al. (2014). Amicoumacin a inhibits translation by stabilizing mRNA interaction with the ribosome. Molecular Cell, 56(4), 531-540. doi:10.1016/j.molcel.2014.09.020.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0023-F410-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-6047-6
Genre: Journal Article

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 Creators:
Polikanov, Y. S., Author
Osterman, I. A., Author
Szal, T., Author
Tashlitsky, V. N., Author
Serebryakova, M. V., Author
Kusochek, P., Author
Bulkley, D., Author
Malanicheva, I. A., Author
Efimenko, T. A., Author
Efremenkova, O. V., Author
Konevega, A. L., Author
Shaw, k.J., Author
Bogdanov, A. A., Author
Rodnina, M. V.1, Author              
Dontsova, O. A., Author
Mankin, A. S., Author
Steitz, T. A., Author
Sergiev, P. V., Author
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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 Abstract: We demonstrate that the antibiotic amicoumacin A (AMI) is a potent inhibitor of protein synthesis. Resistance mutations in helix 24 of the 16S rRNA mapped the AMI binding site to the small ribosomal subunit. The crystal structure of bacterial ribosome in complex with AMI solved at 2.4 Å resolution revealed that the antibiotic makes contacts with universally conserved nucleotides of 16S rRNA in the E site and the mRNA backbone. Simultaneous interactions of AMI with 16S rRNA and mRNA and the in vivo experimental evidence suggest that it may inhibit the progression of the ribosome along mRNA. Consistent with this proposal, binding of AMI interferes with translocation in vitro. The inhibitory action of AMI can be partly compensated by mutations in the translation elongation factor G.

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Language(s): eng - English
 Dates: 2014-10-092014-11-20
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.molcel.2014.09.020
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Title: Molecular Cell
Source Genre: Journal
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Pages: - Volume / Issue: 56 (4) Sequence Number: - Start / End Page: 531 - 540 Identifier: -