Abstract
DNA replication elongation is tightly controlled by histone-modifying enzymes. Our previous studies showed that the histone methytransferase TXR1 (Tetrahymena Trithorax related protein 1) specifically catalyzes H3K27 monomethylation and affects DNA replication elongation in Tetrahymena thermophila. In this study, we investigated whether TXR1 has a substrate preference to the canonical H3 over the replacement variant H3.3. We demonstrated by histone mutagenesis that K27Q mutation in H3.3 further aggravated the replication stress phenotype of K27Q mutation in canonical H3, supporting H3.3 as a physiologically relevant substrate of TXR1. This result is in apparent contrast to the strong preference for canonical H3 recently reported in Arabidopsis homologues ATXR5 and ATXR6, and further corroborates the role of TXR1 in DNA replication.
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Acknowledgements
Our thanks are due to Prof. Weibo Song from Ocean University of China, for his kind help in preparing the draft and illustrations. We also thank Mr. Mingjian Liu, Lab. of Protozoology, Ocean University of China, for providing in vivo and protogal staining pictures of Tetrahymena. This work was supported by the Natural Science Foundation of China (31470064, 31522051 to Shan Gao), the National Institutes of Health (R01- GM087343 to Yifan Liu), AoShan Talents Program supported by Qingdao National Laboratory for Marine Science and Technology (2015ASTP), China and a research grant by Qingdao government (15-12-1-1-jch).
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Zhao, X., Wang, Y., Wang, Y. et al. Histone methyltransferase TXR1 is required for both H3 and H3.3 lysine 27 methylation in the well-known ciliated protist Tetrahymena thermophila . Sci. China Life Sci. 60, 264–270 (2017). https://doi.org/10.1007/s11427-016-0183-1
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DOI: https://doi.org/10.1007/s11427-016-0183-1