HCF-1 Is Cleaved in the Active Site of O-GlcNAc Transferase-Reference-Cited by-同舟云学术

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

Published:2013-12-06 Issue:6163 Volume:342 Page:1235-1239
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Lazarus Michael B.¹²,Jiang Jiaoyang¹,Kapuria Vaibhav³,Bhuiyan Tanja³,Janetzko John²,Zandberg Wesley F.⁴,Vocadlo David J.⁴⁵,Herr Winship³,Walker Suzanne¹

Affiliation:

1. Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA.

2. Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.

3. Center for Integrative Genomics, University of Lausanne, Génopode, 1015 Lausanne, Switzerland.

4. Department of Chemistry, Simon Fraser University, Burnaby, BC V5A 1S6, Canada.

5. Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada.

Abstract

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

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference39 articles.

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