Mammalian Bcnt/Cfdp1, a potential epigenetic factor characterized by an acidic stretch in the disordered N-terminal and Ser phosphorylation in the conserved C-terminal regions
Bioscience Reports, ISSN: 1573-4935, Vol: 35, Issue: 4, Page: e00228-e00228
2015
- 9Citations
- 14Captures
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Metrics Details
- Citations9
- Citation Indexes9
- CrossRef9
- Captures14
- Readers14
- 14
Article Description
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, Ser, 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 Ser 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 Ser phosphorylation in BCNT-C. Furthermore, Bcnt/Cfdp1 is acetylated in vitro by CREB-binding protein (CBP) and four lysine residues including Lys in BCNT-C are also acetylated in vivo, revealing a protein regulated at multiple levels.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84937117807&origin=inward; http://dx.doi.org/10.1042/bsr20150111; http://www.ncbi.nlm.nih.gov/pubmed/26182435; https://portlandpress.com/bioscirep/article/35/4/e00228/56164/Mammalian-Bcnt-Cfdp1-a-potential-epigenetic-factor; http://bioscirep.org/cgi/doi/10.1042/BSR20150111; https://dx.doi.org/10.1042/bsr20150111
Portland Press Ltd.
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