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A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity
Leucyl-tRNA synthetases (LeuRSs) catalyze the linkage of leucine with tRNA(Leu). LeuRS contains a catalysis domain (aminoacylation) and a CP1 domain (editing). CP1 is inserted 35 Å from the aminoacylation domain. Aminoacylation and editing require CP1 to swing to the coordinated conformation. The ne...
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/PMC4138327/ https://www.ncbi.nlm.nih.gov/pubmed/25051973 http://dx.doi.org/10.1261/rna.044404.114 |
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author | Huang, Qian Zhou, Xiao-Long Hu, Qin-Hua Lei, Hui-Yan Fang, Zhi-Peng Yao, Peng Wang, En-Duo |
author_facet | Huang, Qian Zhou, Xiao-Long Hu, Qin-Hua Lei, Hui-Yan Fang, Zhi-Peng Yao, Peng Wang, En-Duo |
author_sort | Huang, Qian |
collection | PubMed |
description | Leucyl-tRNA synthetases (LeuRSs) catalyze the linkage of leucine with tRNA(Leu). LeuRS contains a catalysis domain (aminoacylation) and a CP1 domain (editing). CP1 is inserted 35 Å from the aminoacylation domain. Aminoacylation and editing require CP1 to swing to the coordinated conformation. The neck between the CP1 domain and the aminoacylation domain is defined as the CP1 hairpin. The location of the CP1 hairpin suggests a crucial role in the CP1 swing and domain–domain interaction. Here, the CP1 hairpin of Homo sapiens cytoplasmic LeuRS (hcLeuRS) was deleted or substituted by those from other representative species. Lack of a CP1 hairpin led to complete loss of aminoacylation, amino acid activation, and tRNA binding; however, the mutants retained post-transfer editing. Only the CP1 hairpin from Saccharomyces cerevisiae LeuRS (ScLeuRS) could partly rescue the hcLeuRS functions. Further site-directed mutagenesis indicated that the flexibility of small residues and the charge of polar residues in the CP1 hairpin are crucial for the function of LeuRS. |
format | Online Article Text |
id | pubmed-4138327 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Cold Spring Harbor Laboratory Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-41383272015-09-01 A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity Huang, Qian Zhou, Xiao-Long Hu, Qin-Hua Lei, Hui-Yan Fang, Zhi-Peng Yao, Peng Wang, En-Duo RNA Articles Leucyl-tRNA synthetases (LeuRSs) catalyze the linkage of leucine with tRNA(Leu). LeuRS contains a catalysis domain (aminoacylation) and a CP1 domain (editing). CP1 is inserted 35 Å from the aminoacylation domain. Aminoacylation and editing require CP1 to swing to the coordinated conformation. The neck between the CP1 domain and the aminoacylation domain is defined as the CP1 hairpin. The location of the CP1 hairpin suggests a crucial role in the CP1 swing and domain–domain interaction. Here, the CP1 hairpin of Homo sapiens cytoplasmic LeuRS (hcLeuRS) was deleted or substituted by those from other representative species. Lack of a CP1 hairpin led to complete loss of aminoacylation, amino acid activation, and tRNA binding; however, the mutants retained post-transfer editing. Only the CP1 hairpin from Saccharomyces cerevisiae LeuRS (ScLeuRS) could partly rescue the hcLeuRS functions. Further site-directed mutagenesis indicated that the flexibility of small residues and the charge of polar residues in the CP1 hairpin are crucial for the function of LeuRS. Cold Spring Harbor Laboratory Press 2014-09 /pmc/articles/PMC4138327/ /pubmed/25051973 http://dx.doi.org/10.1261/rna.044404.114 Text en © 2014 Huang 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 Huang, Qian Zhou, Xiao-Long Hu, Qin-Hua Lei, Hui-Yan Fang, Zhi-Peng Yao, Peng Wang, En-Duo A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity |
title | A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity |
title_full | A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity |
title_fullStr | A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity |
title_full_unstemmed | A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity |
title_short | A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity |
title_sort | bridge between the aminoacylation and editing domains of leucyl-trna synthetase is crucial for its synthetic activity |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4138327/ https://www.ncbi.nlm.nih.gov/pubmed/25051973 http://dx.doi.org/10.1261/rna.044404.114 |
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