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Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase

In all organisms, aminoacyl tRNA synthetases covalently attach amino acids to their cognate tRNAs. Many eukaryotic tRNA synthetases have acquired appended domains, whose origin, structure and function are poorly understood. The N-terminal appended domain (NTD) of glutaminyl-tRNA synthetase (GlnRS) i...

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Autores principales: Grant, Thomas D., Snell, Edward H., Luft, Joseph R., Quartley, Erin, Corretore, Stephanie, Wolfley, Jennifer R., Elizabeth Snell, M., Hadd, Andrew, Perona, John J., Phizicky, Eric M., Grayhack, Elizabeth J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3333875/
https://www.ncbi.nlm.nih.gov/pubmed/22180531
http://dx.doi.org/10.1093/nar/gkr1223
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author Grant, Thomas D.
Snell, Edward H.
Luft, Joseph R.
Quartley, Erin
Corretore, Stephanie
Wolfley, Jennifer R.
Elizabeth Snell, M.
Hadd, Andrew
Perona, John J.
Phizicky, Eric M.
Grayhack, Elizabeth J.
author_facet Grant, Thomas D.
Snell, Edward H.
Luft, Joseph R.
Quartley, Erin
Corretore, Stephanie
Wolfley, Jennifer R.
Elizabeth Snell, M.
Hadd, Andrew
Perona, John J.
Phizicky, Eric M.
Grayhack, Elizabeth J.
author_sort Grant, Thomas D.
collection PubMed
description In all organisms, aminoacyl tRNA synthetases covalently attach amino acids to their cognate tRNAs. Many eukaryotic tRNA synthetases have acquired appended domains, whose origin, structure and function are poorly understood. The N-terminal appended domain (NTD) of glutaminyl-tRNA synthetase (GlnRS) is intriguing since GlnRS is primarily a eukaryotic enzyme, whereas in other kingdoms Gln-tRNA(Gln) is primarily synthesized by first forming Glu-tRNA(Gln), followed by conversion to Gln-tRNA(Gln) by a tRNA-dependent amidotransferase. We report a functional and structural analysis of the NTD of Saccharomyces cerevisiae GlnRS, Gln4. Yeast mutants lacking the NTD exhibit growth defects, and Gln4 lacking the NTD has reduced complementarity for tRNA(Gln) and glutamine. The 187-amino acid Gln4 NTD, crystallized and solved at 2.3 Å resolution, consists of two subdomains, each exhibiting an extraordinary structural resemblance to adjacent tRNA specificity-determining domains in the GatB subunit of the GatCAB amidotransferase, which forms Gln-tRNA(Gln). These subdomains are connected by an apparent hinge comprised of conserved residues. Mutation of these amino acids produces Gln4 variants with reduced affinity for tRNA(Gln), consistent with a hinge-closing mechanism proposed for GatB recognition of tRNA. Our results suggest a possible origin and function of the NTD that would link the phylogenetically diverse mechanisms of Gln-tRNA(Gln) synthesis.
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spelling pubmed-33338752012-04-23 Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase Grant, Thomas D. Snell, Edward H. Luft, Joseph R. Quartley, Erin Corretore, Stephanie Wolfley, Jennifer R. Elizabeth Snell, M. Hadd, Andrew Perona, John J. Phizicky, Eric M. Grayhack, Elizabeth J. Nucleic Acids Res Structural Biology In all organisms, aminoacyl tRNA synthetases covalently attach amino acids to their cognate tRNAs. Many eukaryotic tRNA synthetases have acquired appended domains, whose origin, structure and function are poorly understood. The N-terminal appended domain (NTD) of glutaminyl-tRNA synthetase (GlnRS) is intriguing since GlnRS is primarily a eukaryotic enzyme, whereas in other kingdoms Gln-tRNA(Gln) is primarily synthesized by first forming Glu-tRNA(Gln), followed by conversion to Gln-tRNA(Gln) by a tRNA-dependent amidotransferase. We report a functional and structural analysis of the NTD of Saccharomyces cerevisiae GlnRS, Gln4. Yeast mutants lacking the NTD exhibit growth defects, and Gln4 lacking the NTD has reduced complementarity for tRNA(Gln) and glutamine. The 187-amino acid Gln4 NTD, crystallized and solved at 2.3 Å resolution, consists of two subdomains, each exhibiting an extraordinary structural resemblance to adjacent tRNA specificity-determining domains in the GatB subunit of the GatCAB amidotransferase, which forms Gln-tRNA(Gln). These subdomains are connected by an apparent hinge comprised of conserved residues. Mutation of these amino acids produces Gln4 variants with reduced affinity for tRNA(Gln), consistent with a hinge-closing mechanism proposed for GatB recognition of tRNA. Our results suggest a possible origin and function of the NTD that would link the phylogenetically diverse mechanisms of Gln-tRNA(Gln) synthesis. Oxford University Press 2012-04 2011-12-16 /pmc/articles/PMC3333875/ /pubmed/22180531 http://dx.doi.org/10.1093/nar/gkr1223 Text en © The Author(s) 2011. 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 unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Structural Biology
Grant, Thomas D.
Snell, Edward H.
Luft, Joseph R.
Quartley, Erin
Corretore, Stephanie
Wolfley, Jennifer R.
Elizabeth Snell, M.
Hadd, Andrew
Perona, John J.
Phizicky, Eric M.
Grayhack, Elizabeth J.
Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase
title Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase
title_full Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase
title_fullStr Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase
title_full_unstemmed Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase
title_short Structural conservation of an ancient tRNA sensor in eukaryotic glutaminyl-tRNA synthetase
title_sort structural conservation of an ancient trna sensor in eukaryotic glutaminyl-trna synthetase
topic Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3333875/
https://www.ncbi.nlm.nih.gov/pubmed/22180531
http://dx.doi.org/10.1093/nar/gkr1223
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