Title : In vivo putative O-GlcNAcylation of human
SCP1 and evidence for possible role of its N-terminal disordered structure
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)
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. SCP1, , SCP1, In vivo putative O-GlcNAcylation, -
- 5. Ser41, , -, the O-GlcNAc modification site, Ser41 residue
- 5. hSCP1, , hSCP1, the O-GlcNAc modification site, -
Output(Part-Of) (sent_index,
protein,
site):
- 1. RNA polymerase II, domain
- 1. subunit, domain
- 5. hSCP1, Ser41 residue
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 5. hSCP1, the O-GlcNAc modification site, Ser41 residue