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Title: The crystal structure of human GlnRS provides basis for the development of neurological disorders

Abstract

Cytosolic glutaminyl-tRNA synthetase (GlnRS) is the singular enzyme responsible for translation of glutamine codons. Compound heterozygous mutations in GlnRS cause severe brain disorders by a poorly understood mechanism. Herein, we present crystal structures of the wild type and two pathological mutants of human GlnRS, which reveal, for the first time, the domain organization of the intact enzyme and the structure of the functionally important N-terminal domain (NTD). Pathological mutations mapping in the NTD alter the domain structure, and decrease catalytic activity and stability of GlnRS, whereas missense mutations in the catalytic domain induce misfolding of the enzyme. Our results suggest that the reduced catalytic efficiency and a propensity of GlnRS mutants to misfold trigger the disease development. As a result, this report broadens the spectrum of brain pathologies elicited by protein misfolding and provides a paradigm for understanding the role of mutations in aminoacyl-tRNA synthetases in neurological diseases. Keywords

Authors:
 [1];  [2];  [3];  [3];  [3];  [2];  [1]
+ Show Author Affiliations
  1. Univ. of Illinois, Chicago, IL (United States)
  2. The Univ. of Texas, Houston, TX (United States)
  3. National Institute of Health, Bethesda, MD (United States)
Publication Date:
Research Org.:
Univ. of Texas, Houston, TX (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); Michigan Economic Development Corporation; Michigan Technology Tri-Corridor; NCI; National Institute of General Medical Sciences (NIGMS) of the National Institutes of Health (NIH); The University of Texas, Health Science Center at Houston
OSTI Identifier:
1262023
Grant/Contract Number:  
AC02-06CH11357
Resource Type:
Accepted Manuscript
Journal Name:
Nucleic Acids Research
Additional Journal Information:
Journal Volume: 44; Journal Issue: 7; Journal ID: ISSN 0305-1048
Publisher:
Oxford University Press
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; transfer-rna-synthetase; spinal-cord involvement; marie-tooth-disease; pontocerebellar hypoplasia; brain-stem; perrault syndrome; hearing-loss; mutations; gene; evolution

Citation Formats

Ognjenovic, Jana, Wu, Jiang, Matthies, Doreen, Baxa, Ulrich, Subramaniam, Sriram, Ling, Jiqiang, and Simonovic, Miljan. The crystal structure of human GlnRS provides basis for the development of neurological disorders. United States: N. p., 2016. Web. doi:10.1093/nar/gkw082.
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Ognjenovic, Jana, Wu, Jiang, Matthies, Doreen, Baxa, Ulrich, Subramaniam, Sriram, Ling, Jiqiang, & Simonovic, Miljan. The crystal structure of human GlnRS provides basis for the development of neurological disorders. United States. https://doi.org/10.1093/nar/gkw082
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Ognjenovic, Jana, Wu, Jiang, Matthies, Doreen, Baxa, Ulrich, Subramaniam, Sriram, Ling, Jiqiang, and Simonovic, Miljan. Wed . "The crystal structure of human GlnRS provides basis for the development of neurological disorders". United States. https://doi.org/10.1093/nar/gkw082. https://www.osti.gov/servlets/purl/1262023.
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@article{osti_1262023,
title = {The crystal structure of human GlnRS provides basis for the development of neurological disorders},
author = {Ognjenovic, Jana and Wu, Jiang and Matthies, Doreen and Baxa, Ulrich and Subramaniam, Sriram and Ling, Jiqiang and Simonovic, Miljan},
abstractNote = {Cytosolic glutaminyl-tRNA synthetase (GlnRS) is the singular enzyme responsible for translation of glutamine codons. Compound heterozygous mutations in GlnRS cause severe brain disorders by a poorly understood mechanism. Herein, we present crystal structures of the wild type and two pathological mutants of human GlnRS, which reveal, for the first time, the domain organization of the intact enzyme and the structure of the functionally important N-terminal domain (NTD). Pathological mutations mapping in the NTD alter the domain structure, and decrease catalytic activity and stability of GlnRS, whereas missense mutations in the catalytic domain induce misfolding of the enzyme. Our results suggest that the reduced catalytic efficiency and a propensity of GlnRS mutants to misfold trigger the disease development. As a result, this report broadens the spectrum of brain pathologies elicited by protein misfolding and provides a paradigm for understanding the role of mutations in aminoacyl-tRNA synthetases in neurological diseases. Keywords},
doi = {10.1093/nar/gkw082},
journal = {Nucleic Acids Research},
number = 7,
volume = 44,
place = {United States},
year = {Wed Feb 10 00:00:00 EST 2016},
month = {Wed Feb 10 00:00:00 EST 2016}
}
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https://doi.org/10.1093/nar/gkw082
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