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1H, 13C and 15N resonance assignment of WHEP domains of human glutamyl-prolyl tRNA synthetase

1H, 13C and 15N resonance assignment of WHEP domains of human glutamyl-prolyl tRNA synthetase Human bifunctional glutamyl-prolyl tRNA synthetase (EPRS) contains three WHEP domains (R123) linking two catalytic domains. These three WHEP domains have been shown to be involved in protein–protein and protein–nucleic acid interactions. In translational control of gene expression, R12 repeats is known to interact with 3′UTR element in mRNAs of inflammatory gene for translational control mechanisms. While, R23 repeats interacts with NSAP1, which inhibits mRNA binding. Here we present the NMR chemical shift assignments for R12 (128 amino acids) as a 14 kDa recombinant protein and whole WHEP domains R123 (208 amino acids) as a 21 kDa recombinant protein. 97 % of backbone and 98 % of side-chain assignments have been completed in R12 analysis and 93 and 92 % of backbone and side-chain, respectively, assignments have been completed in R123 analysis based upon triple-resonance experiments. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

1H, 13C and 15N resonance assignment of WHEP domains of human glutamyl-prolyl tRNA synthetase

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Publisher
Springer Journals
Copyright
Copyright © 2013 by Springer Science+Business Media Dordrecht
Subject
Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-013-9538-7
pmid
24378977
Publisher site
See Article on Publisher Site

Abstract

Human bifunctional glutamyl-prolyl tRNA synthetase (EPRS) contains three WHEP domains (R123) linking two catalytic domains. These three WHEP domains have been shown to be involved in protein–protein and protein–nucleic acid interactions. In translational control of gene expression, R12 repeats is known to interact with 3′UTR element in mRNAs of inflammatory gene for translational control mechanisms. While, R23 repeats interacts with NSAP1, which inhibits mRNA binding. Here we present the NMR chemical shift assignments for R12 (128 amino acids) as a 14 kDa recombinant protein and whole WHEP domains R123 (208 amino acids) as a 21 kDa recombinant protein. 97 % of backbone and 98 % of side-chain assignments have been completed in R12 analysis and 93 and 92 % of backbone and side-chain, respectively, assignments have been completed in R123 analysis based upon triple-resonance experiments.

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Dec 31, 2013

References