Literature summary for 3.5.1.98 extracted from

Vendrell, A.; Martinez-Pastor, M.; Gonzalez-Novo, A.; Pascual-Ahuir, A.; Sinclair, D.A.; Proft, M.; Posas, F.
Sir2 histone deacetylase prevents programmed cell death caused by sustained activation of the Hog1 stress-activated protein kinase (2011), EMBO Rep., 12, 1062-1068.

Search for more literature for 3.5.1.98

Organism

Organism	UniProt	Comment	Textmining

Expression

Organism	Comment	Expression
Saccharomyces cerevisiae	mutations of the SCF-CDC4 ubiquitin ligase complex suppress cell death by preventing the degradation of Msn2 and Msn4 transcription factors. Accumulation of transcription factors Msn2 and Msn4 leads to the induction of PNC1, which is an activator of the Sir2 histone acetylase	up

General Information

General Information	Comment	Organism
physiological function	Sir2 is involved in protection against Hog1-induced cell death and can suppress Hog1-induced reactive oxygen species accumulation. Therefore, cell death seems to be dictated by the balance of reactive oxygen species induced by Hog1 and the protective effect of Sir2. Prolonged activation of stress-activated protein kinase leads to cell death, by causing accumulation of reactive oxygen species. Mutations of the SCF-CDC4 ubiquitin ligase complex suppress cell death by preventing the degradation of Msn2 and Msn4 transcription factors. Accumulation of transcription factors Msn2 and Msn4 leads to the induction of PNC1, which is an activator of the Sir2 histone acetylase	Saccharomyces cerevisiae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)