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Mammalian Bcnt/Cfdp1, a potential epigenetic factor characterized by an acidic stretch in the disordered N-terminal and Ser250 phosphorylation in the conserved C-terminal regions
https://repo.qst.go.jp/records/47288
https://repo.qst.go.jp/records/47288016be903-480f-4210-bfb9-98559debc1d8
Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2015-09-15 | |||||
タイトル | ||||||
タイトル | Mammalian Bcnt/Cfdp1, a potential epigenetic factor characterized by an acidic stretch in the disordered N-terminal and Ser250 phosphorylation in the conserved C-terminal regions | |||||
言語 | ||||||
言語 | eng | |||||
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資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
アクセス権 | ||||||
アクセス権 | metadata only access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
著者 |
Iwashita, Shintaro
× Iwashita, Shintaro× Suzuki, Takehiro× 安田, 武嗣× Nakashima, Kentaro× Sakamoto, Taiichi× Kohno, Toshiyuki× Takahashi, Ichiro× Kobayashi, Takayasu× Ohno-Iwashita, Yoshiko× Imajoh-Ohmi, Shinobu× Song, Si-Young× 安田 武嗣 |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | The BCNT (Bucentaur) superfamily is classified by an uncharacteristic conserved sequence of ∼80 amino acids (aa) at the C-terminus, BCNT-C (the conserved C-terminal region of Bcnt/Cfdp1). Whereas the yeast Swc5 and Drosophila Yeti homologues play crucial roles in chromatin remodelling organization, mammalian Bcnt/Cfdp1 (craniofacial developmental protein 1) remains poorly understood. The protein, which lacks cysteine, is largely disordered and comprises an acidic N-terminal region, a lysine/glutamic acid/proline-rich 40 aa sequence and BCNT-C. It shows complex mobility on SDS/PAGE at ∼50 kDa, whereas its calculated molecular mass is ∼33 kDa. To characterize this mobility discrepancy and the effects of post-translational modifications (PTMs), we expressed various deleted His– Bcnt in E. coli and HEK cells and found that an acidic stretch in the N-terminal region is a main cause of the gel shift. Exogenous BCNT/CFDP1 constitutively expressed in HEK clones appears as a doublet at 49 and 47 kDa, slower than the protein expressed in Escherichia coli but faster than the endogenous protein on SDS/PAGE. Among seven in vivo phosphorylation sites, Ser250, which resides in a region between disordered and ordered regions in BCNT-C, is heavily phosphorylated and detected predominantly in the 49 kDa band. Together with experiments involving treatment with phosphatases and Ser250 substitutions, the results indicate that the complex behaviour of Bcnt/Cfdp1 on SDS/PAGE is caused mainly by an acidic stretch in the N-terminal region and Ser250 phosphorylation in BCNT-C. Furthermore, Bcnt/Cfdp1 is acetylated in vitro by CREB-binding protein (CBP) and four lysine residues including Lys268 in BCNT-C are also acetylated in vivo, revealing a protein regulated at multiple levels. |
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書誌情報 |
Bioscience Reports 巻 35, 号 4, p. e00228, 発行日 2015-06 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0144-8463 | |||||
DOI | ||||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1042/BSR20150111 |