Plasmodium falciparum Sir2 is an NAD+-Dependent Deacetylase and an Acetyllysine-Dependent and Acetyllysine-Independent NAD+ Glycohydrolase
نویسندگان
چکیده
منابع مشابه
SIRT3, a human SIR2 homologue, is an NAD-dependent deacetylase localized to mitochondria.
The SIR2 (silent information regulator 2) gene family has diverse functions in yeast including gene silencing, DNA repair, cell-cycle progression, and chromosome fidelity in meiosis and aging. Human homologues, termed sirtuins, are highly conserved but are of unknown function. We previously identified a large imprinted gene domain on 11p15.5 and investigated the 11p15.5 sirtuin SIRT3. Although ...
متن کاملStructural basis for the NAD-dependent deacetylase mechanism of Sir2.
The NAD-dependent histone/protein deacetylase activity of Sir2 (silent information regulator 2) accounts for its diverse biological roles including gene silencing, DNA damage repair, cell cycle regulation, and life span extension. We provide crystallographic evidence that 2'-O-acetyl ADP-ribose is the reaction product that is formed at the active site of Sir2 from the 2.6-A co-crystal structure...
متن کاملThe Leishmania infantum cytosolic SIR2-related protein 1 (LiSIR2RP1) is an NAD+ -dependent deacetylase and ADP-ribosyltransferase.
Proteins of the SIR2 (Silent Information Regulator 2) family are characterized by a conserved catalytic domain that exerts unique NAD(+)-dependent deacetylase activity on histones and various other cellular substrates. Previous reports from us have identified a Leishmania infantum gene encoding a cytosolic protein termed LiSIR2RP1 (Leishmania infantum SIR2-related protein 1) that belongs to the...
متن کاملSir2-Related Protein 1 from Leishmania amazonensis is a glycosylated NAD+-dependent deacetylase.
Sirtuin proteins form a family of NAD+-dependent protein deacetylases that are considered potential drug targets against parasites. Here, we present the first characterization of a sirtuin orthologue from Leishmania amazonensis, an aetiological agent of American tegumentary leishmaniasis that has been the subject of many studies focused in the development of therapeutic approaches. The protein ...
متن کاملhSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase
DNA damage-induced acetylation of p53 protein leads to its activation and either growth arrest or apoptosis. We show here that the protein product of the gene hSIR2(SIRT1), the human homolog of the S. cerevisiae Sir2 protein known to be involved in cell aging and in the response to DNA damage, binds and deacetylates the p53 protein with a specificity for its C-terminal Lys382 residue, modificat...
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ژورنال
عنوان ژورنال: Biochemistry
سال: 2008
ISSN: 0006-2960,1520-4995
DOI: 10.1021/bi800767t