Two Conserved Cysteine Residues Are Required for the Masculinizing Activity of the Silkworm Masc Protein.

The Journal of Biological Chemistry
Susumu KatsumaToru Shimada

Abstract

We have recently discovered that the Masculinizer (Masc) gene encodes a CCCH tandem zinc finger protein, which controls both masculinization and dosage compensation in the silkworm Bombyx mori. In this study, we attempted to identify functional regions or residues that are required for the masculinizing activity of the Masc protein. We constructed a series of plasmids that expressed the Masc derivatives and transfected them into a B. mori ovary-derived cell line, BmN-4. To assess the masculinizing activity of the Masc derivatives, we investigated the splicing patterns of B. mori doublesex (Bmdsx) and the expression levels of B. mori IGF-II mRNA-binding protein, a splicing regulator of Bmdsx, in Masc cDNA-transfected BmN-4 cells. We found that two zinc finger domains are not required for the masculinizing activity. We also identified that the C-terminal 288 amino acid residues are sufficient for the masculinizing activity of the Masc protein. Further detailed analyses revealed that two cysteine residues, Cys-301 and Cys-304, in the highly conserved region among lepidopteran Masc proteins are essential for the masculinizing activity in BmN-4 cells. Finally, we showed that Masc is a nuclear protein, but its nuclear localization is...Continue Reading

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Citations

Jul 12, 2019·FEBS Open Bio·Susumu KatsumaTakashi Kiuchi
May 16, 2018·Proceedings of the Japan Academy. Series B, Physical and Biological Sciences·Susumu KatsumaKen Sahara
Apr 12, 2020·International Journal of Molecular Sciences·Yao WangXing-Fu Zha
Mar 7, 2021·Genes·Xu YangYongping Huang
Aug 28, 2021·International Journal of Molecular Sciences·Zhongyuan DengXianchun Li

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