RRC ID 36144
著者 Katsuma S, Sugano Y, Kiuchi T, Shimada T.
タイトル Two Conserved Cysteine Residues Are Required for the Masculinizing Activity of the Silkworm Masc Protein.
ジャーナル J Biol Chem
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 not tightly associated with the masculinizing activity.
巻・号 290(43)
ページ 26114-24
公開日 2015-10-23
DOI 10.1074/jbc.M115.685362
PII S0021-9258(20)49589-4
PMID 26342076
PMC PMC4646263
MeSH Amino Acid Sequence Animals Base Sequence Bombyx / metabolism* Cell Line Conserved Sequence Cysteine / metabolism* Female Insect Proteins / metabolism Insect Proteins / physiology* Sequence Homology, Amino Acid Sequence Homology, Nucleic Acid
IF 4.238
引用数 13
WOS 分野 BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
カイコ