@article{oai:repo.qst.go.jp:00047288,
 author = {Iwashita, Shintaro and Suzuki, Takehiro and 安田, 武嗣 and Nakashima, Kentaro and Sakamoto, Taiichi and Kohno, Toshiyuki and Takahashi, Ichiro and Kobayashi, Takayasu and Ohno-Iwashita, Yoshiko and Imajoh-Ohmi, Shinobu and Song, Si-Young and 安田 武嗣},
 issue = {4},
 journal = {Bioscience Reports},
 month = {Jun},
 note = {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.},
 title = {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},
 volume = {35},
 year = {2015}
}