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Mammalian Bcnt/Cfdp1, a potential epigenetic factor characterized by an acidic stretch in the disordered N-terminal and S250 phosphorylation in the conserved C-terminal regions

ABSTRACT: The function of mammalian Bcnt protein is poorly understood yet, though Bcnt homologs (yeast Swc5 and Dorsophila Yeti) play crucial roles in chromatin remodeling organization. In this study, we found that mammalian Bcnt protein shows unusual mobility on SDS-PAGE and is acetylated in vitro by CREB-binding protein. Therefore, we analyzed Bcnt protein by LC-MSMS to characterize the protein structure containing post-translational modifications (phosphorylation and acetylation) which may be the cause of this unusual mobility.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Takehiro Suzuki

PROVIDER: MSV000080755 | MassIVE | Wed Mar 29 06:59:00 BST 2017

SECONDARY ACCESSION(S): PXD002228

REPOSITORIES: MassIVE

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Mammalian Bcnt/Cfdp1, a potential epigenetic factor characterized by an acidic stretch in the disordered N-terminal and S250 phosphorylation in the conserved C-terminal regions

Project description:The function of mammalian Bcnt protein is poorly understood yet, though Bcnt homologs (yeast Swc5 and Dorsophila Yeti) play crucial roles in chromatin remodeling organization. In this study, we found that mammalian Bcnt protein shows unusual mobility on SDS-PAGE and is acetylated in vitro by CREB-binding protein. Therefore, we analyzed Bcnt protein by LC-MSMS to characterize the protein structure containing post-translational modifications (phosphorylation and acetylation) which may be the cause of this unusual mobility.

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