Cargando…

Ribosomal protein uS19 mutants reveal its role in coordinating ribosome structure and function

Prior studies identified allosteric information pathways connecting functional centers in the large ribosomal subunit to the decoding center in the small subunit through the B1a and B1b/c intersubunit bridges in yeast. In prokaryotes a single SSU protein, uS13, partners with H38 (the A-site finger)...

Descripción completa

Detalles Bibliográficos
Autores principales: Bowen, Alicia M, Musalgaonkar, Sharmishtha, Moomau, Christine A, Gulay, Suna P, Mirvis, Mary, Dinman, Jonathan D
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Taylor & Francis 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721500/
https://www.ncbi.nlm.nih.gov/pubmed/26824029
http://dx.doi.org/10.1080/21690731.2015.1117703
_version_ 1782411237227757568
author Bowen, Alicia M
Musalgaonkar, Sharmishtha
Moomau, Christine A
Gulay, Suna P
Mirvis, Mary
Dinman, Jonathan D
author_facet Bowen, Alicia M
Musalgaonkar, Sharmishtha
Moomau, Christine A
Gulay, Suna P
Mirvis, Mary
Dinman, Jonathan D
author_sort Bowen, Alicia M
collection PubMed
description Prior studies identified allosteric information pathways connecting functional centers in the large ribosomal subunit to the decoding center in the small subunit through the B1a and B1b/c intersubunit bridges in yeast. In prokaryotes a single SSU protein, uS13, partners with H38 (the A-site finger) and uL5 to form the B1a and B1b/c bridges respectively. In eukaryotes, the SSU component was split into 2 separate proteins during the course of evolution. One, also known as uS13, participates in B1b/c bridge with uL5 in eukaryotes. The other, called uS19 is the SSU partner in the B1a bridge with H38. Here, polyalanine mutants of uS19 involved in the uS19/uS13 and the uS19/H38 interfaces were used to elucidate the important amino acid residues involved in these intersubunit communication pathways. Two key clusters of amino acids were identified: one located at the junction between uS19 and uS13, and a second that appears to interact with the distal tip of H38. Biochemical analyses reveal that these mutations shift the ribosomal rotational equilibrium toward the unrotated state, increasing ribosomal affinity for tRNAs in the P-site and for ternary complex in the A-site, and inhibit binding of the translocase, eEF2. These defects in turn affect specific aspects of translational fidelity. These findings suggest that uS19 plays a critical role as a conduit of information exchange between the large and small ribosomal subunits directly through the B1a, and indirectly through the B1b/c bridges.
format Online
Article
Text
id pubmed-4721500
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher Taylor & Francis
record_format MEDLINE/PubMed
spelling pubmed-47215002016-01-28 Ribosomal protein uS19 mutants reveal its role in coordinating ribosome structure and function Bowen, Alicia M Musalgaonkar, Sharmishtha Moomau, Christine A Gulay, Suna P Mirvis, Mary Dinman, Jonathan D Translation (Austin) Research Paper Prior studies identified allosteric information pathways connecting functional centers in the large ribosomal subunit to the decoding center in the small subunit through the B1a and B1b/c intersubunit bridges in yeast. In prokaryotes a single SSU protein, uS13, partners with H38 (the A-site finger) and uL5 to form the B1a and B1b/c bridges respectively. In eukaryotes, the SSU component was split into 2 separate proteins during the course of evolution. One, also known as uS13, participates in B1b/c bridge with uL5 in eukaryotes. The other, called uS19 is the SSU partner in the B1a bridge with H38. Here, polyalanine mutants of uS19 involved in the uS19/uS13 and the uS19/H38 interfaces were used to elucidate the important amino acid residues involved in these intersubunit communication pathways. Two key clusters of amino acids were identified: one located at the junction between uS19 and uS13, and a second that appears to interact with the distal tip of H38. Biochemical analyses reveal that these mutations shift the ribosomal rotational equilibrium toward the unrotated state, increasing ribosomal affinity for tRNAs in the P-site and for ternary complex in the A-site, and inhibit binding of the translocase, eEF2. These defects in turn affect specific aspects of translational fidelity. These findings suggest that uS19 plays a critical role as a conduit of information exchange between the large and small ribosomal subunits directly through the B1a, and indirectly through the B1b/c bridges. Taylor & Francis 2015-11-18 /pmc/articles/PMC4721500/ /pubmed/26824029 http://dx.doi.org/10.1080/21690731.2015.1117703 Text en © 2015 The Author(s). Published with license by Taylor & Francis 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 unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.
spellingShingle Research Paper
Bowen, Alicia M
Musalgaonkar, Sharmishtha
Moomau, Christine A
Gulay, Suna P
Mirvis, Mary
Dinman, Jonathan D
Ribosomal protein uS19 mutants reveal its role in coordinating ribosome structure and function
title Ribosomal protein uS19 mutants reveal its role in coordinating ribosome structure and function
title_full Ribosomal protein uS19 mutants reveal its role in coordinating ribosome structure and function
title_fullStr Ribosomal protein uS19 mutants reveal its role in coordinating ribosome structure and function
title_full_unstemmed Ribosomal protein uS19 mutants reveal its role in coordinating ribosome structure and function
title_short Ribosomal protein uS19 mutants reveal its role in coordinating ribosome structure and function
title_sort ribosomal protein us19 mutants reveal its role in coordinating ribosome structure and function
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721500/
https://www.ncbi.nlm.nih.gov/pubmed/26824029
http://dx.doi.org/10.1080/21690731.2015.1117703
work_keys_str_mv AT bowenaliciam ribosomalproteinus19mutantsrevealitsroleincoordinatingribosomestructureandfunction
AT musalgaonkarsharmishtha ribosomalproteinus19mutantsrevealitsroleincoordinatingribosomestructureandfunction
AT moomauchristinea ribosomalproteinus19mutantsrevealitsroleincoordinatingribosomestructureandfunction
AT gulaysunap ribosomalproteinus19mutantsrevealitsroleincoordinatingribosomestructureandfunction
AT mirvismary ribosomalproteinus19mutantsrevealitsroleincoordinatingribosomestructureandfunction
AT dinmanjonathand ribosomalproteinus19mutantsrevealitsroleincoordinatingribosomestructureandfunction