Smith Jeffrey
Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Jordan Hall, Box 800733, Charlottesville, VA 22908, USA.
Trends Cell Biol. 2002 Sep;12(9):404-6. doi: 10.1016/s0962-8924(02)02342-5.
Members of the evolutionarily conserved silent information regulator 2 (Sir2) protein family are nicotinamide adenine dinucleotide (NAD(+))-dependent histone deacetylases. In yeast, the founding Sir2 protein is known to function in transcriptional silencing processes through the deacetylation of histones H3 and H4, thus setting up a repressive chromatin structure. Yeast and Caenorhabditis elegans Sir2 are also involved in regulating the life span of these organisms. Until recently, the function of mammalian Sir2 family members was completely unknown. However, several recent studies have now determined a remarkable function for the human SIRT1 protein, which is the closest human homolog of yeast Sir2. SIRT1 specifically associates with the p53 tumor suppressor protein and deacetylates it, resulting in negative regulation of p53-mediated transcriptional activation. Importantly, p53 deacetylation by SIRT1 also prevents cellular senescence and apoptosis induced by DNA damage and stress.
进化上保守的沉默信息调节因子2(Sir2)蛋白家族的成员是烟酰胺腺嘌呤二核苷酸(NAD(+))依赖性组蛋白脱乙酰酶。在酵母中,最初发现的Sir2蛋白通过组蛋白H3和H4的去乙酰化作用参与转录沉默过程,从而建立起一种抑制性染色质结构。酵母和秀丽隐杆线虫的Sir2也参与调节这些生物体的寿命。直到最近,哺乳动物Sir2家族成员的功能还完全未知。然而,最近的几项研究现已确定了人类SIRT1蛋白的显著功能,它是酵母Sir2在人类中最接近的同源物。SIRT1特异性地与p53肿瘤抑制蛋白结合并使其去乙酰化,导致对p53介导的转录激活的负调控。重要的是,SIRT1介导的p53去乙酰化还可防止DNA损伤和应激诱导的细胞衰老和凋亡。