O-linked N-acetylglucosamine suppresses thermal aggregation of Sp1 - PubMed (original) (raw)
. 2006 Aug 21;580(19):4645-52.
doi: 10.1016/j.febslet.2006.07.040. Epub 2006 Jul 21.
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- PMID: 16879824
- DOI: 10.1016/j.febslet.2006.07.040
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O-linked N-acetylglucosamine suppresses thermal aggregation of Sp1
Ki-Hong Lim et al. FEBS Lett. 2006.
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Abstract
We demonstrate that O-linked N-acetylglucosamine (O-GlcNAc), a ubiquitous protein modification in eukaryotes, suppresses thermal inactivation of Sp1 transcription factor. 6-Diazo-5-oxonorleucine treatment or O-GlcNAcase overexpression, which reduced O-GlcNAc levels on Sp1, deteriorated thermal stability of Sp1 and O-GlcNAc modified molecules of Sp1 resist thermal aggregation in vitro. We also showed that heat-induced elevation of heat shock protein 70 was facilitated by Sp1 but blunted under low O-GlcNAc levels, suggesting that O-GlcNAc might upregulate the expression of heat shock protein 70 through thermoprotection of Sp1, which eventually enhanced cellular thermotolerance.
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