HCF-1 is cleaved in the active site of O-GlcNAc transferase.

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Auteurs
Date

2013

Type de document
Périmètre
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Serveur académique Lausannois

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Ce document est lié à :
info:eu-repo/semantics/altIdentifier/doi/10.1126/science.1243990

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/pmid/24311690

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/eissn/1095-9203

Ce document est lié à :
info:eu-repo/semantics/altIdentifier/urn/urn:nbn:ch:serval-BIB_0C03172DF49E3

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Serveur Académique Lausannois

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Université de Lausanne et CHUV

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info:eu-repo/semantics/openAccess , Copying allowed only for non-profit organizations , https://serval.unil.ch/disclaimer

Mots-clés 0

Amino Acid Motifs; Amino Acid Substitution; Catalytic Domain; Crystallography, X-Ray; Glycosylation; Host Cell Factor C1/chemistry; Host Cell Factor C1/metabolism; Humans; Hydrogen Bonding; Models, Molecular; N-Acetylglucosaminyltransferases/chemistry; N-Acetylglucosaminyltransferases/metabolism; Protein Conformation; Protein Structure, Tertiary; Proteolysis; Pyrrolidonecarboxylic Acid/metabolism; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/metabolism; Uridine Diphosphate N-Acetylglucosamine/chemistry; Uridine Diphosphate N-Acetylglucosamine/metabolism

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Glycation

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M.B. Lazarus et al., « HCF-1 is cleaved in the active site of O-GlcNAc transferase. », Serveur académique Lausannois, ID : 10.1126/science.1243990

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Host cell factor-1 (HCF-1), a transcriptional co-regulator of human cell-cycle progression, undergoes proteolytic maturation in which any of six repeated sequences is cleaved by the nutrient-responsive glycosyltransferase, O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT). We report that the tetratricopeptide-repeat domain of O-GlcNAc transferase binds the carboxyl-terminal portion of an HCF-1 proteolytic repeat such that the cleavage region lies in the glycosyltransferase active site above uridine diphosphate-GlcNAc. The conformation is similar to that of a glycosylation-competent peptide substrate. Cleavage occurs between cysteine and glutamate residues and results in a pyroglutamate product. Conversion of the cleavage site glutamate into serine converts an HCF-1 proteolytic repeat into a glycosylation substrate. Thus, protein glycosylation and HCF-1 cleavage occur in the same active site.

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