1 H, 13 C and 15 N resonance assignments of Q38FZ4, hypothetical protein from Trypanosoma brucei
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ARTICLE
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H, 13C and 15N resonance assignments of Q38FZ4, hypothetical protein from Trypanosoma brucei Rui Wang1 · Jiahai Zhang2 · Shanhui Liao2 · Xiaoming Tu2 Received: 17 March 2020 / Accepted: 30 May 2020 © Springer Nature B.V. 2020
Abstract Q38FZ4 (UniProt accession number), is an 85-residue hypothetical protein from Trypanosoma brucei (T. brucei). Q38FZ4, which might be specific among the trypanosomatid genomes, shares low sequence similarity with mammal proteins and also has an essential function in the growth of T. brucei. Here we report the resonance assignments and secondary structure analysis of Q38FZ4 from T. brucei, which will lay the foundation for the protein structure determination and function elucidation. Keywords Q38FZ4 · T. brucei · hypothetical protein · Resonance assignment
Biological context Trypanosoma brucei is a unicellular flagellated eukaryote causing neglected tropical diseases including sleeping sickness in human and nagana in cattle. So far, there are no vaccines to prevent or treat these illnesses, which still led to 60 million people at risk and ∼ 30,000 deaths per year in the developing countries in sub-Saharan Africa (Simarro et al. 2008). T. brucei which diverged early from the eukaryotic lineage, has many different characteristics compared with other well-studied eukaryotic organisms (Embley and Martin 2006). The genome sequences of T. brucei were reported in 2005, which revealed that over half of protein-coding genes were annotated “hypothetical” (Berriman et al. 2005). Most of these hypothetical proteins with unknown functions are essential for the growth of T. brucei (Alsford et al. 2011). Therefore, studies on the hypothetical proteins of T. brucei can increase the knowledge about the cellular biology and
pathogenesis of the parasite, which will also provide new perspectives for drug development. Q38FZ4 is a conserved and specific hypothetical protein in T. brucei which has been proved to be essential in both bloodstream and procyclic forms of the parasite, as well as in differentiation of the procyclic to bloodstream form (Alsford et al. 2011). In addition, it exhibits low primary sequence homology with proteins from other organisms. When searching with its primary sequence to find homologies, only several trypanosome hypothetical proteins of unknown function match. All these features will make Q38FZ4 a potential target for new drug development against trypanosomatid parasites. So determining the structure of Q38FZ4 is desirable for drug screening and providing insights on Q38FZ4 function. To gain insight into the structure and function of Q38FZ4 protein, we analyzed the NMR data of Q38FZ4 to establish its structural information. Here, the backbone and side-chain 1 H, 13C and 15N resonance assignments of Q38FZ4 from T. brucei are determined.
* Xiaoming Tu [email protected]
Methods and experiments
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Department of Anthropotomy and Histoembryology, Medical College, Henan University of Science and Technology, Luoyang 471023, Henan, People’s Republic of China
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