The conserved threonine-rich region of the HCF-1_PRO repeat activates promiscuous OGT:UDP-GlcNAc glycosylation and proteolysis activities.

ABSTRACT: O-Linked GlcNAc transferase (OGT) possesses dual glycosyltransferase-protease activities. OGT thereby stably glycosylates serines and threonines of numerous proteins and, via a transient glutamate glycosylation, cleaves a single known substrate-the so-called HCF-1_PRO repeat of the transcriptional co-regulator host-cell factor 1 (HCF-1). Here, we probed the relationship between these distinct glycosylation and proteolytic activities. For proteolysis, the HCF-1_PRO repeat possesses an important extended threonine-rich region that is tightly bound by the OGT tetratricopeptide-repeat (TPR) region. We report that linkage of this HCF-1_PRO-repeat, threonine-rich region to heterologous substrate sequences also potentiates robust serine glycosylation with the

SUBMITTER: Kapuria V 

PROVIDER: S-EPMC6240873 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature