Cited 4 time in webofscience Cited 3 time in scopus

In vivo putative O-GlcNAcylation of human SCP1 and evidence for possible role of its N-terminal disordered structure

Title
In vivo putative O-GlcNAcylation of human SCP1 and evidence for possible role of its N-terminal disordered structure
Authors
Koo, JH[Koo, Jae Hyung]Bahk, YY[Bahk, Young Yil]
DGIST Authors
Koo, JH[Koo, Jae Hyung]
Issue Date
2014-10-31
Citation
BMB Reports, 47(10), 593-598
Type
Article
Article Type
Article
Keywords
3T3 Cell LineAnimalAnimalsChemistryCTD Phosphatase SCP1CTDSP1 Protein, HumanEnhanced Green Fluorescent ProteinEnzyme SpecificityGlycosylationGreen Fluorescent ProteinGreen Fluorescent ProteinsHumanHumansInducible Mammalian Expression SystemIntrinsically Disordered ProteinIntrinsically Disordered ProteinsMammaliaMetabolismMiceMouseNIH 3T3 CellsNuclear ProteinNuclear ProteinsO-GlcNAcPhosphoprotein PhosphatasePhosphoprotein PhosphatasesPost-Translational ModificationProtein ProcessingProtein Processing, Post-TranslationalSerineSubstrate Specificity
ISSN
1976-6696
Abstract
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.
URI
http://hdl.handle.net/20.500.11750/3016
DOI
10.5483/BMBRep.2014.47.10.144
Publisher
Korean Society for Molecular and Cellular Biology
Related Researcher
  • Author Koo, Jae Hyung The Koo Lab - ChemoReception Laboratory(CRLab)
  • Research Interests
Files:
There are no files associated with this item.
Collection:
New BiologyETC1. Journal Articles


qrcode mendeley

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE