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The N-terminal extension of S12 influences small ribosomal subunit assembly in Escherichia coli
The small subunit (SSU) of the ribosome of E. coli consists of a core of ribosomal RNA (rRNA) surrounded peripherally by ribosomal proteins (r-proteins). Ten of the 15 universally conserved SSU r-proteins possess nonglobular regions called extensions. The N-terminal noncanonically structured extensi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory Press
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3923127/ https://www.ncbi.nlm.nih.gov/pubmed/24442609 http://dx.doi.org/10.1261/rna.042432.113 |
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author | Calidas, Deepika Lyon, Hiram Culver, Gloria M. |
author_facet | Calidas, Deepika Lyon, Hiram Culver, Gloria M. |
author_sort | Calidas, Deepika |
collection | PubMed |
description | The small subunit (SSU) of the ribosome of E. coli consists of a core of ribosomal RNA (rRNA) surrounded peripherally by ribosomal proteins (r-proteins). Ten of the 15 universally conserved SSU r-proteins possess nonglobular regions called extensions. The N-terminal noncanonically structured extension of S12 traverses from the solvent to intersubunit surface of the SSU and is followed by a more C-terminal globular region that is adjacent to the decoding center of the SSU. The role of the globular region in maintaining translational fidelity is well characterized, but a role for the S12 extension in SSU structure and function is unknown. We examined the effect of stepwise truncation of the extension of S12 in SSU assembly and function in vitro and in vivo. Examination of in vitro assembly in the presence of sequential N-terminal truncated variants of S12 reveals that N-terminal deletions of greater than nine amino acids exhibit decreased tRNA-binding activity and altered 16S rRNA architecture particularly in the platform of the SSU. While wild-type S12 expressed from a plasmid can rescue a genomic deletion of the essential gene for S12, rpsl; N-terminal deletions of S12 exhibit deleterious phenotypic consequences. Partial N-terminal deletions of S12 are slow growing and cold sensitive. Strains bearing these truncations as the sole copy of S12 have increased levels of free SSUs and immature 16S rRNA as compared with the wild-type S12. These differences are hallmarks of SSU biogenesis defects, indicating that the extension of S12 plays an important role in SSU assembly. |
format | Online Article Text |
id | pubmed-3923127 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-39231272015-03-01 The N-terminal extension of S12 influences small ribosomal subunit assembly in Escherichia coli Calidas, Deepika Lyon, Hiram Culver, Gloria M. RNA Articles The small subunit (SSU) of the ribosome of E. coli consists of a core of ribosomal RNA (rRNA) surrounded peripherally by ribosomal proteins (r-proteins). Ten of the 15 universally conserved SSU r-proteins possess nonglobular regions called extensions. The N-terminal noncanonically structured extension of S12 traverses from the solvent to intersubunit surface of the SSU and is followed by a more C-terminal globular region that is adjacent to the decoding center of the SSU. The role of the globular region in maintaining translational fidelity is well characterized, but a role for the S12 extension in SSU structure and function is unknown. We examined the effect of stepwise truncation of the extension of S12 in SSU assembly and function in vitro and in vivo. Examination of in vitro assembly in the presence of sequential N-terminal truncated variants of S12 reveals that N-terminal deletions of greater than nine amino acids exhibit decreased tRNA-binding activity and altered 16S rRNA architecture particularly in the platform of the SSU. While wild-type S12 expressed from a plasmid can rescue a genomic deletion of the essential gene for S12, rpsl; N-terminal deletions of S12 exhibit deleterious phenotypic consequences. Partial N-terminal deletions of S12 are slow growing and cold sensitive. Strains bearing these truncations as the sole copy of S12 have increased levels of free SSUs and immature 16S rRNA as compared with the wild-type S12. These differences are hallmarks of SSU biogenesis defects, indicating that the extension of S12 plays an important role in SSU assembly. Cold Spring Harbor Laboratory Press 2014-03 /pmc/articles/PMC3923127/ /pubmed/24442609 http://dx.doi.org/10.1261/rna.042432.113 Text en © 2014 Calidas et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/3.0/ 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 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/. |
spellingShingle | Articles Calidas, Deepika Lyon, Hiram Culver, Gloria M. The N-terminal extension of S12 influences small ribosomal subunit assembly in Escherichia coli |
title | The N-terminal extension of S12 influences small ribosomal subunit assembly in Escherichia coli |
title_full | The N-terminal extension of S12 influences small ribosomal subunit assembly in Escherichia coli |
title_fullStr | The N-terminal extension of S12 influences small ribosomal subunit assembly in Escherichia coli |
title_full_unstemmed | The N-terminal extension of S12 influences small ribosomal subunit assembly in Escherichia coli |
title_short | The N-terminal extension of S12 influences small ribosomal subunit assembly in Escherichia coli |
title_sort | n-terminal extension of s12 influences small ribosomal subunit assembly in escherichia coli |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3923127/ https://www.ncbi.nlm.nih.gov/pubmed/24442609 http://dx.doi.org/10.1261/rna.042432.113 |
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