Modification of the RpoS network with a synthetic small RNA

Modification of the RpoS network with a synthetic small RNA

Translation of the sigma factor RpoS is activated by DsrA, RprA and ArcA, three small non-coding sRNAs (sRNA) that expose the ribosome-binding site (RBS) by opening up an inhibitory loop. In the RpoS network, no sRNAs have been found to pair with the RBS, a most common sRNA target site in bacteria....

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Main Authors: Jin, Ye, Wu, Jianting, Li, Yannan, Cai, Zhiming, Huang, Jian-Dong
Format: Online
Language:English
Published: Oxford University Press 2013
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3783183/
id pubmed-3783183
recordtype oai_dc
spelling pubmed-37831832013-09-30 Modification of the RpoS network with a synthetic small RNA Jin, Ye Wu, Jianting Li, Yannan Cai, Zhiming Huang, Jian-Dong RNA Translation of the sigma factor RpoS is activated by DsrA, RprA and ArcA, three small non-coding sRNAs (sRNA) that expose the ribosome-binding site (RBS) by opening up an inhibitory loop. In the RpoS network, no sRNAs have been found to pair with the RBS, a most common sRNA target site in bacteria. Here, we generate Ribo-0, an artificial sRNA, which represses rpoS translation by pairing with the RBS. Ribo-0 bypasses the RNA chaperon Hfq but requires the RBS to be loosely blocked. Ribo-0 interacts with DsrA and reshapes the RpoS network. Specifically, in the intact RpoS network, DsrA activates rpoS translation by freeing up the RBS. In the modified RpoS network where Ribo-0 is introduced, the DsrA-caused RBS exposure facilitates Ribo-0 binding, thereby strengthening Ribo-0 inhibition. In other words, Ribo-0 changes DsrA from an activator to an accomplice for repressing rpoS translation. This work presents an artificial mechanism of rpoS regulation, reveals mutual effects of native and synthetic players and demonstrates genetic context-dependency of their functions. Oxford University Press 2013-09 2013-07-09 /pmc/articles/PMC3783183/ /pubmed/23842672 http://dx.doi.org/10.1093/nar/gkt604 Text en © The Author(s) 2013. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Jin, Ye
Wu, Jianting
Li, Yannan
Cai, Zhiming
Huang, Jian-Dong
spellingShingle Jin, Ye
Wu, Jianting
Li, Yannan
Cai, Zhiming
Huang, Jian-Dong
Modification of the RpoS network with a synthetic small RNA
author_facet Jin, Ye
Wu, Jianting
Li, Yannan
Cai, Zhiming
Huang, Jian-Dong
author_sort Jin, Ye
title Modification of the RpoS network with a synthetic small RNA
title_short Modification of the RpoS network with a synthetic small RNA
title_full Modification of the RpoS network with a synthetic small RNA
title_fullStr Modification of the RpoS network with a synthetic small RNA
title_full_unstemmed Modification of the RpoS network with a synthetic small RNA
title_sort modification of the rpos network with a synthetic small rna
description Translation of the sigma factor RpoS is activated by DsrA, RprA and ArcA, three small non-coding sRNAs (sRNA) that expose the ribosome-binding site (RBS) by opening up an inhibitory loop. In the RpoS network, no sRNAs have been found to pair with the RBS, a most common sRNA target site in bacteria. Here, we generate Ribo-0, an artificial sRNA, which represses rpoS translation by pairing with the RBS. Ribo-0 bypasses the RNA chaperon Hfq but requires the RBS to be loosely blocked. Ribo-0 interacts with DsrA and reshapes the RpoS network. Specifically, in the intact RpoS network, DsrA activates rpoS translation by freeing up the RBS. In the modified RpoS network where Ribo-0 is introduced, the DsrA-caused RBS exposure facilitates Ribo-0 binding, thereby strengthening Ribo-0 inhibition. In other words, Ribo-0 changes DsrA from an activator to an accomplice for repressing rpoS translation. This work presents an artificial mechanism of rpoS regulation, reveals mutual effects of native and synthetic players and demonstrates genetic context-dependency of their functions.
publisher Oxford University Press
publishDate 2013
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3783183/
_version_ 1612014254091665408

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