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Updated: Mar 23, 2026

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
Published on: January 22, 2019
Solution structure of TbTFIIS2-1 PWWP domain from Trypanosoma brucei
Rui Wang1, Jiahai Zhang1, Shanhui Liao1
1Hefei National Laboratory for Physical Sciences at Microscale, and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People's Republic of China.
Abstract:
TbTFIIS2-1, one of the two TFIIS homologues of Trypanosome brucei (T. brucei), cooperates with TbTFIIS1 in regulating transcription in T. brcuei. Structurally divergent from other TFIIS homologues from higher organisms, TbTFIIS2-1 contains an additional N-terminal PWWP domain besides other three conserved domains, which may imply potential role of TbTFIIS2-1 in transcription regulation. Here, we determined the solution structure of PWWP domain of TbTFIIS2-1 by NMR spectroscopy, which was the first solution structure of PWWP domain solved in trypanosomatid. In spite of poor sequence similarity between PWWP domains, this domain of TbTFIIS2-1 adopts a conserved 3D-structure, which contains a five-stranded β-barrel and a C-terminal α-helix. Furthermore, we found that TbTFIIS2-1 PWWP domain may be a protein-protein interaction module without the ability of DNA recognition and methyl-group interaction. Proteins 2016; 84:912-919. © 2016 Wiley Periodicals, Inc.
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