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P2‐308: Developmental regulation of protein O‐GlcNAcylation, O‐GlcNAc transferase, and O‐GlcNAcase in mammalian brain
Author(s) -
Li Xiaojing,
Gong ChengXin
Publication year - 2011
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2011.05.1186
Subject(s) - threonine , transferase , serine , developmental profile , hippocampus , cerebral cortex , cortex (anatomy) , biology , immunohistochemistry , staining , microbiology and biotechnology , biochemistry , chemistry , phosphorylation , enzyme , neuroscience , endocrinology , genetics , immunology
tants in order to determine regions within the 5’-UTR which influence the translation efficiency of ADAM10. Successive deletion of the first part of the ADAM10 5’-UTR resulted in a significant increase in ADAM10 protein expression, arguing that this part of the 5’-UTR contains inhibitory elements. Using CD-spectroscopy, we identified a G-quadruplex motif, which forms a very stable secondary structure within the first half of the ADAM10 5’-UTR. Mutation of this G-quadruplex motif results in enhanced ADAM10 expression. Conclusions: We provide evidence that a 30 nucleotide long G-rich region within the first portion of the ADAM10 5’UTR is able to form an extremely stable intramolecular G-quadruplex secondary structure which contributes to the inhibitory effect of the 5’-UTR on the translation of ADAM10.