SIRT2
La sirtuina deacetilasi-2 NAD dipendente è un enzima è codificata nell'uomo dal gene SIRT2.[1][2][3]
Questo gene codifica un enzima proteico della famiglia delle sirtuine omologo all'enzima proteico del lievito Sir2. I membri della famiglia delle sirtuine sono caratterizzati da un dominio chiave e vengono classificati in quattro classi distinte. Gli studi suggeriscono che le sirtuine umane possono funzionare come proteine intracellulari di regolazione dell'attività mono-ADP-ribosiltransferasi. La proteina codificata da questo gene è inclusa nella classe I della famiglia delle sirtuine. Vi sono due variazioni trascrizionali dovute a splicing alternativo del gene.[3]
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Organismi modello[modifica]
Le funzioni biochimiche delle sirtuine umane non sono ancora state del tutto chiarite, tuttavia, nel lievito le sirtuine proteiche sono note per la capacità di regolare il silenziamento epigenetico del gene e per la capacità di reprimere la ricombinazione del DNA ricombinante.
Note[modifica]
- ^ Afshar G, Murnane JP (agosto 1999). Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2. Gene 234 (1): 161–8. DOI:10.1016/S0378-1119(99)00162-6. PMID 10393250.
- ^ Frye RA (luglio 1999). Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity. Biochem Biophys Res Commun 260 (1): 273–9. DOI:10.1006/bbrc.1999.0897. PMID 10381378.
- ^ a b Entrez Gene: SIRT2 sirtuin (silent mating type information regulation 2 homolog) 2 (S. cerevisiae)
Bibliografia[modifica]
Riviste[modifica]
- Maruyama K, Sugano S (1994). Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene 138 (1–2): 171–4. DOI:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Andersson B (1996). A "double adaptor" method for improved shotgun library construction. Anal. Biochem. 236 (1): 107–13. DOI:10.1006/abio.1996.0138. PMID 8619474.
- Yu W (1997). Large-Scale Concatenation cDNA Sequencing. Genome Res. 7 (4): 353–8. DOI:10.1101/gr.7.4.353. PMID 9110174.
- Suzuki Y (1997). Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene 200 (1–2): 149–56. DOI:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Frye RA (2000). Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273 (2): 793–8. DOI:10.1006/bbrc.2000.3000. PMID 10873683.
- Hu RM (2000). Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. DOI:10.1073/pnas.160270997. PMID 10931946.
- Finnin MS, Donigian JR, Pavletich NP (2001). Structure of the histone deacetylase SIRT2. Nat. Struct. Biol. 8 (7): 621–5. DOI:10.1038/89668. PMID 11427894.
- Grozinger CM (2001). Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening. J. Biol. Chem. 276 (42): 38837–43. DOI:10.1074/jbc.M106779200. PMID 11483616.
- Borra MT (2002). Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases. J. Biol. Chem. 277 (15): 12632–41. DOI:10.1074/jbc.M111830200. PMID 11812793.
- De Smet C (2002). A novel seven transmembrane receptor induced during the early steps of astrocyte differentiation identified by differential expression. J. Neurochem. 81 (3): 575–88. DOI:10.1046/j.1471-4159.2002.00847.x. PMID 12065666.
- Strausberg RL (2003). Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. DOI:10.1073/pnas.242603899. PMID 12477932.
- North BJ (2003). The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase. Mol. Cell 11 (2): 437–44. DOI:10.1016/S1097-2765(03)00038-8. PMID 12620231.
- Dryden SC (2003). Role for Human SIRT2 NAD-Dependent Deacetylase Activity in Control of Mitotic Exit in the Cell Cycle. Mol. Cell. Biol. 23 (9): 3173–85. DOI:10.1128/MCB.23.9.3173-3185.2003. PMID 12697818.
- Fulco M (2003). Sir2 regulates skeletal muscle differentiation as a potential sensor of the redox state. Mol. Cell 12 (1): 51–62. DOI:10.1016/S1097-2765(03)00226-0. PMID 12887892.
- Hiratsuka M (2003). Proteomics-based identification of differentially expressed genes in human gliomas: down-regulation of SIRT2 gene. Biochem. Biophys. Res. Commun. 309 (3): 558–66. DOI:10.1016/j.bbrc.2003.08.029. PMID 12963026.
- Ota T (2004). Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat. Genet. 36 (1): 40–5. DOI:10.1038/ng1285. PMID 14702039.
- van der Horst A (2004). FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1). J. Biol. Chem. 279 (28): 28873–9. DOI:10.1074/jbc.M401138200. PMID 15126506.
- Bae NS, Swanson MJ, Vassilev A, Howard BH (2005). Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10. J. Biochem. 135 (6): 695–700. DOI:10.1093/jb/mvh084. PMID 15213244.
Testi[modifica]
- Stanley Leonard Robbins; Vinay Kumar; Abul K. Abbas; Ramzi S. Cotran; Nelson Fausto, Robbins and Cotran pathologic basis of disease, Elsevier srl, 2010, 41–. ISBN 978-1-4160-3121-5
- Giuseppe Guglielmi; Francesco Schiavon; Teresa Cammarota, Radiologia Geriatrica, Springer, 6 luglio 2006, 56–. ISBN 978-88-470-0485-6