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Regulation of the rplY gene encoding 5S rRNA binding protein L25 in Escherichia coli and related bacteria
Ribosomal protein (r-protein) L25 is one of the three r-proteins (L25, L5, L18) that interact with 5S rRNA in eubacteria. Specific binding of L25 with a certain domain of 5S r-RNA, a so-called loop E, has been studied in detail, but information about regulation of L25 synthesis has remained totally...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4408793/ https://www.ncbi.nlm.nih.gov/pubmed/25749694 http://dx.doi.org/10.1261/rna.047381.114 |
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author | Aseev, Leonid V. Bylinkina, Natalia S. Boni, Irina V. |
author_facet | Aseev, Leonid V. Bylinkina, Natalia S. Boni, Irina V. |
author_sort | Aseev, Leonid V. |
collection | PubMed |
description | Ribosomal protein (r-protein) L25 is one of the three r-proteins (L25, L5, L18) that interact with 5S rRNA in eubacteria. Specific binding of L25 with a certain domain of 5S r-RNA, a so-called loop E, has been studied in detail, but information about regulation of L25 synthesis has remained totally lacking. In contrast to the rplE (L5) and rplR (L18) genes that belong to the polycistronic spc-operon and are regulated at the translation level by r-protein S8, the rplY (L25) gene forms an independent transcription unit. The main goal of this work was to study the regulation of the rplY expression in vivo. We show that the rplY promoter is down-regulated by ppGpp and its cofactor DksA in response to amino acid starvation. At the level of translation, the rplY expression is subjected to the negative feedback control. The 5′-untranslated region of the rplY mRNA comprises specific sequence/structure features, including an atypical SD-like sequence, which are highly conserved in a subset of gamma-proteobacterial families. Despite the lack of a canonical SD element, the rplY’-‘lacZ single-copy reporter showed unusually high translation efficiency. Expression of the rplY gene in trans decreased the translation yield, indicating the mechanism of autogenous repression. Site-directed mutagenesis of the rplY 5′ UTR revealed an important role of the conserved elements in the translation control. Thus, the rplY expression regulation represents one more example of regulatory pathways that control ribosome biogenesis in Escherichia coli and related bacteria. |
format | Online Article Text |
id | pubmed-4408793 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-44087932016-05-01 Regulation of the rplY gene encoding 5S rRNA binding protein L25 in Escherichia coli and related bacteria Aseev, Leonid V. Bylinkina, Natalia S. Boni, Irina V. RNA Articles Ribosomal protein (r-protein) L25 is one of the three r-proteins (L25, L5, L18) that interact with 5S rRNA in eubacteria. Specific binding of L25 with a certain domain of 5S r-RNA, a so-called loop E, has been studied in detail, but information about regulation of L25 synthesis has remained totally lacking. In contrast to the rplE (L5) and rplR (L18) genes that belong to the polycistronic spc-operon and are regulated at the translation level by r-protein S8, the rplY (L25) gene forms an independent transcription unit. The main goal of this work was to study the regulation of the rplY expression in vivo. We show that the rplY promoter is down-regulated by ppGpp and its cofactor DksA in response to amino acid starvation. At the level of translation, the rplY expression is subjected to the negative feedback control. The 5′-untranslated region of the rplY mRNA comprises specific sequence/structure features, including an atypical SD-like sequence, which are highly conserved in a subset of gamma-proteobacterial families. Despite the lack of a canonical SD element, the rplY’-‘lacZ single-copy reporter showed unusually high translation efficiency. Expression of the rplY gene in trans decreased the translation yield, indicating the mechanism of autogenous repression. Site-directed mutagenesis of the rplY 5′ UTR revealed an important role of the conserved elements in the translation control. Thus, the rplY expression regulation represents one more example of regulatory pathways that control ribosome biogenesis in Escherichia coli and related bacteria. Cold Spring Harbor Laboratory Press 2015-05 /pmc/articles/PMC4408793/ /pubmed/25749694 http://dx.doi.org/10.1261/rna.047381.114 Text en © 2015 Aseev et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/4.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/. |
spellingShingle | Articles Aseev, Leonid V. Bylinkina, Natalia S. Boni, Irina V. Regulation of the rplY gene encoding 5S rRNA binding protein L25 in Escherichia coli and related bacteria |
title | Regulation of the rplY gene encoding 5S rRNA binding protein L25 in Escherichia coli and related bacteria |
title_full | Regulation of the rplY gene encoding 5S rRNA binding protein L25 in Escherichia coli and related bacteria |
title_fullStr | Regulation of the rplY gene encoding 5S rRNA binding protein L25 in Escherichia coli and related bacteria |
title_full_unstemmed | Regulation of the rplY gene encoding 5S rRNA binding protein L25 in Escherichia coli and related bacteria |
title_short | Regulation of the rplY gene encoding 5S rRNA binding protein L25 in Escherichia coli and related bacteria |
title_sort | regulation of the rply gene encoding 5s rrna binding protein l25 in escherichia coli and related bacteria |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4408793/ https://www.ncbi.nlm.nih.gov/pubmed/25749694 http://dx.doi.org/10.1261/rna.047381.114 |
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