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O‐linked N ‐acetylglucosamine suppresses thermal aggregation of Sp1
Author(s) -
Lim Ki-Hong,
Chang Hyo-Ihl
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.07.040
Subject(s) - heat shock protein , chemistry , downregulation and upregulation , in vitro , hsp70 , sp1 transcription factor , diazo , transcription (linguistics) , hsp90 , microbiology and biotechnology , biochemistry , biology , gene expression , promoter , gene , medicinal chemistry , linguistics , philosophy
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.