Shin ChinHo, Hwang Geum-Sook, Ahn Hee-Chul, Kim Sunghoon, Kim Key-Sun
University of Science and Technology, Gajeong-ro 217, Yuseong-gu, Taejon, 305-333, Republic of Korea.
Biomol NMR Assign. 2015 Apr;9(1):25-30. doi: 10.1007/s12104-013-9538-7. Epub 2013 Dec 31.
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.
人双功能谷氨酰胺 - 脯氨酸tRNA合成酶（EPRS）包含连接两个催化结构域的三个WHEP结构域（R123）。已证明这三个WHEP结构域参与蛋白质 - 蛋白质和蛋白质 - 核酸相互作用。在基因表达的翻译控制中，已知R12重复序列与炎症基因mRNA中的3'UTR元件相互作用以实现翻译控制机制。而R23重复序列与NSAP1相互作用，NSAP1会抑制mRNA结合。在此，我们给出了作为14 kDa重组蛋白的R12（128个氨基酸）以及作为21 kDa重组蛋白的整个WHEP结构域R123（208个氨基酸）的核磁共振化学位移归属。基于三共振实验，在R12分析中已完成97%的主链和98%的侧链归属，在R123分析中分别完成了93%的主链和92%的侧链归属。
