HCF-1 Is Cleaved in the Active Site of O-GlcNAc Transferase

• DOI: 10.1126/science.1243990
• Publication Date: 2013-12-05T19:18:05Z
• Authors: Michael B. Lazarus; Jiaoyang Jiang; Vaibhav Kapuria; Tanja Bhuiyan; John Janetzko; Wesley F. Zandberg; David J. Vocadlo; Winship Herr; Suzanne Walker
• Keywords: Transferase; Cleavage (geology); Cleave; Site-directed mutagenesis

Dual-Duty Active Site O-linked N-acetylglucosamine transferase (OGT) catalyzes the addition of (GlcNac) to serine or threonine residues, influencing localization and function proteins. Because its activity is sensitive nutrient uridine diphosphate (UDP)–GlcNac, OGT has been proposed regulate cellular responses status. Recently, in presence UDP-GlcNac was shown cleave host cell factor–1 (HCF-1), a transcriptional coregulator human cell-cycle progression. This cleavage required for HCF-1 maturation. Through combination structural, biochemical, mutagenesis studies, Lazarus et al. (p. 1235 ) show that both glycosylation occur active site. Cleavage occurs between cysteine glutamine converts into which can then be glycosylated.