dc.contributor.author	Meydan, Sezen
dc.contributor.author	Marks, James
dc.contributor.author	Klepacki, Dorota
dc.contributor.author	Sharma, Virag
dc.contributor.author	Baranov, Pavel V.
dc.contributor.author	Firth, Andrew E.
dc.contributor.author	Margus, Tonu
dc.contributor.author	Kefi, Amira
dc.contributor.author	Vázquez-Laslop, Nora
dc.contributor.author	Mankin, Alexander S.
dc.contributor.funder	National Science Foundation	en
dc.contributor.funder	Science Foundation Ireland	en
dc.contributor.funder	Health Research Board	en
dc.contributor.funder	Wellcome Trust	en
dc.date.accessioned	2019-05-20T08:59:19Z
dc.date.available	2019-05-20T08:59:19Z
dc.date.issued	2019-03-20
dc.date.updated	2019-05-20T08:35:46Z
dc.description.abstract	The use of alternative translation initiation sites enables production of more than one protein from a single gene, thereby expanding the cellular proteome. Although several such examples have been serendipitously found in bacteria, genome-wide mapping of alternative translation start sites has been unattainable. We found that the antibiotic retapamulin specifically arrests initiating ribosomes at start codons of the genes. Retapamulin-enhanced Ribo-seq analysis (Ribo-RET) not only allowed mapping of conventional initiation sites at the beginning of the genes, but strikingly, it also revealed putative internal start sites in a number of Escherichia coli genes. Experiments demonstrated that the internal start codons can be recognized by the ribosomes and direct translation initiation in vitro and in vivo. Proteins, whose synthesis is initiated at internal in-frame and out-of-frame start sites, can be functionally important and contribute to the “alternative” bacterial proteome. The internal start sites may also play regulatory roles in gene expression.	en
dc.description.sponsorship	National Science Foundation (MCB 1615851); SFI-HRB-Wellcome Trust Biomedical Research Partnership (210692/Z/18/Z); Wellcome Trust (106207)	en
dc.description.status	Peer reviewed	en
dc.description.version	Accepted Version	en
dc.format.mimetype	application/pdf	en
dc.identifier.citation	Meydan, S., Marks, J., Klepacki, D., Sharma, V., Baranov, P. V., Firth, A. E., Margus, T., Kefi, A., Vázquez-Laslop, N. and Mankin, A. S. (2019) 'Retapamulin-assisted ribosome profiling reveals the alternative bacterial proteome', Molecular Cell, 74(3), pp. 481-493. doi: 10.1016/j.molcel.2019.02.017	en
dc.identifier.doi	10.1016/j.molcel.2019.02.017	en
dc.identifier.eissn	1097-4164
dc.identifier.endpage	493	en
dc.identifier.issn	1097-2765
dc.identifier.issued	3	en
dc.identifier.journaltitle	Molecular Cell	en
dc.identifier.startpage	481	en
dc.identifier.uri	https://hdl.handle.net/10468/7933
dc.identifier.volume	74	en
dc.language.iso	en	en
dc.publisher	Elsevier Inc.	en
dc.relation.uri	http://www.sciencedirect.com/science/article/pii/S1097276519301078
dc.rights	© 2019, Elsevier Inc. All rights reserved. This manuscript version is made available under the CC BY-NC-ND 4.0 license.	en
dc.rights.uri	https://creativecommons.org/licenses/by-nc-nd/4.0/	en
dc.subject	Ribosome profiling	en
dc.subject	Translation initiation	en
dc.subject	Retapamulin	en
dc.subject	Alternative initiation	en
dc.subject	Internal genes	en
dc.title	Retapamulin-assisted ribosome profiling reveals the alternative bacterial proteome	en
dc.type	Article (peer-reviewed)	en

Retapamulin-assisted ribosome profiling reveals the alternative bacterial proteome

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