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In vivo putative O-GlcNAcylation of human SCP1 and evidence for possible role of its N-terminal disordered structure
- In vivo putative O-GlcNAcylation of human SCP1 and evidence for possible role of its N-terminal disordered structure
- Koo, JH[Koo, Jae Hyung]; Bahk, YY[Bahk, Young Yil]
- DGIST Authors
- Koo, JH[Koo, Jae Hyung]
- Issue Date
- BMB Reports, 47(10), 593-598
- Article Type
- 3T3 Cell Line; Animal; Animals; Chemistry; CTD Phosphatase SCP1; CTDSP1 Protein, Human; Enhanced Green Fluorescent Protein; Enzyme Specificity; Glycosylation; Green Fluorescent Protein; Green Fluorescent Proteins; Human; Humans; Inducible Mammalian Expression System; Intrinsically Disordered Protein; Intrinsically Disordered Proteins; Mammalia; Metabolism; Mice; Mouse; NIH 3T3 Cells; Nuclear Protein; Nuclear Proteins; O-GlcNAc; Phosphoprotein Phosphatase; Phosphoprotein Phosphatases; Post-Translational Modification; Protein Processing; Protein Processing, Post-Translational; Serine; Substrate Specificity
- RNA polymerase II carboxyl-terminal domain (RNAPII CTD) phosphatases are responsible for the dephosphorylation of the C-terminal domain of the small subunit of RNAPII in eukaryotes. Recently, we demonstrated the identification of several interacting partners with human small CTD phosphatase1 (hSCP1) and the substrate specificity to delineate an appearance of the dephosphorylation catalyzed by SCP1. In this study, using the established cells for inducibly expressing hSCP1 proteins, we monitored the modification of β-O-linked N-acetylglucosamine (O-GlcNAc). O-GlcNAcylation is one of the most common post-translational modifications (PTMs). To gain insight into the PTM of hSCP1, we used the Western blot, immunoprecipitation, succinylayed wheat germ agglutininprecipitation, liquid chromatography-mass spectrometry analyses, and site-directed mutagenesis and identified the Ser41 residue of hSCP1 as the O-GlcNAc modification site. These results suggest that hSCP1 may be an O-GlcNAcylated protein in vivo, and its N-terminus may function a possible role in the PTM, providing a scaffold for binding the protein(s). © 2014 by the The Korean Society for Biochemistry and Molecular Biology.
- Korean Society for Molecular and Cellular Biology
- Related Researcher
Koo, Jae Hyung
The Koo Lab - ChemoReception Laboratory(CRLab)
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