O-linked N-acetylglucosamine suppresses thermal aggregation of Sp1

Ki Hong Lim, Hyo-Ihl Chang

Research output: Contribution to journalArticle

31 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)4645-4652
Number of pages8
JournalFEBS Letters
Volume580
Issue number19
DOIs
Publication statusPublished - 2006 Aug 21

Fingerprint

Acetylglucosamine
HSP70 Heat-Shock Proteins
Agglomeration
Hot Temperature
Sp1 Transcription Factor
Thermodynamic stability
Eukaryota
Molecules
Up-Regulation
Proteins

Keywords

  • Heat shock protein 70
  • O-GlcNAc
  • Sp1
  • Thermal aggregation
  • Thermotolerance

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

O-linked N-acetylglucosamine suppresses thermal aggregation of Sp1. / Lim, Ki Hong; Chang, Hyo-Ihl.

In: FEBS Letters, Vol. 580, No. 19, 21.08.2006, p. 4645-4652.

Research output: Contribution to journalArticle

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