Sirtuin 1

From Wikipedia, the free encyclopedia

Sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae)

Identifiers

SIRT1; SIR2L1

External IDs

OMIM: 604479 MGI: 2135607 HomoloGene: 56556

Gene ontology
Molecular Function:	• DNA binding • NAD+ ADP-ribosyltransferase activity • zinc ion binding • transcription repressor activity • hydrolase activity • NAD-dependent histone deacetylase activity • metal ion binding
Cellular Component:	• nucleus • chromatin silencing complex
Biological Process:	• ovulation (sensu Mammalia) • chromatin silencing • transcription • regulation of transcription, DNA-dependent • protein amino acid ADP-ribosylation • apoptosis • multicellular organismal development • spermatogenesis • striated muscle development • negative regulation of transcription • histone deacetylation • cell differentiation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_012238 (mRNA)
NP_036370 (protein)

XM_975350 (mRNA)
XP_980444 (protein)

Location

Chr 10: 69.31 - 69.35 Mb

Chr 10: 62.71 - 62.73 Mb

Pubmed search

[1]

[2]

Sirtuin 1 (also known as SIRT1 or silent mating type information regulation 2 homolog S. cerevisiae) stands for sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae), referring to the fact that its sirtuin homolog (biological equivalent across species) in yeast (S. cerevisiae) is Sir2. SIRT1 is an enzyme which deacetylates proteins that contribute to cellular regulation (reaction to stressors, longevity) [3]. ^[1]

This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family.^[1]

1 References
2 Further reading
3 See also
4 External links

[edit] References

^ ^a ^b Entrez Gene: SIRT1 sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae).

[edit] Further reading

Frye RA (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.
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.
Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.154701. PMID 11230166.
Luo J, Nikolaev AY, Imai S, et al. (2001). "Negative control of p53 by Sir2alpha promotes cell survival under stress.". Cell 107 (2): 137–48. PMID 11672522.
Vaziri H, Dessain SK, Ng Eaton E, et al. (2001). "hSIR2(SIRT1) functions as an NAD-dependent p53 deacetylase.". Cell 107 (2): 149–59. PMID 11672523.
Langley E, Pearson M, Faretta M, et al. (2002). "Human SIR2 deacetylates p53 and antagonizes PML/p53-induced cellular senescence.". EMBO J. 21 (10): 2383–96. doi:10.1093/emboj/21.10.2383. PMID 12006491.
Bitterman KJ, Anderson RM, Cohen HY, et al. (2003). "Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1.". J. Biol. Chem. 277 (47): 45099–107. doi:10.1074/jbc.M205670200. PMID 12297502.
Travers H, Spotswood HT, Moss PA, Turner BM (2002). "Human CD34+ hematopoietic progenitor cells hyperacetylate core histones in response to sodium butyrate, but not trichostatin A.". Exp. Cell Res. 280 (2): 149–58. PMID 12413881.
Strausberg RL, Feingold EA, Grouse LH, et al. (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.
Takata T, Ishikawa F (2003). "Human Sir2-related protein SIRT1 associates with the bHLH repressors HES1 and HEY2 and is involved in HES1- and HEY2-mediated transcriptional repression.". Biochem. Biophys. Res. Commun. 301 (1): 250–7. PMID 12535671.
Senawong T, Peterson VJ, Avram D, et al. (2003). "Involvement of the histone deacetylase SIRT1 in chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2-mediated transcriptional repression.". J. Biol. Chem. 278 (44): 43041–50. doi:10.1074/jbc.M307477200. PMID 12930829.
Howitz KT, Bitterman KJ, Cohen HY, et al. (2003). "Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan.". Nature 425 (6954): 191–6. doi:10.1038/nature01960. PMID 12939617.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Brunet A, Sweeney LB, Sturgill JF, et al. (2004). "Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase.". Science 303 (5666): 2011–5. doi:10.1126/science.1094637. PMID 14976264.
Motta MC, Divecha N, Lemieux M, et al. (2004). "Mammalian SIRT1 represses forkhead transcription factors.". Cell 116 (4): 551–63. PMID 14980222.
van der Horst A, Tertoolen LG, de Vries-Smits LM, et al. (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.
Yeung F, Hoberg JE, Ramsey CS, et al. (2004). "Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase.". EMBO J. 23 (12): 2369–80. doi:10.1038/sj.emboj.7600244. PMID 15152190.
Deloukas P, Earthrowl ME, Grafham DV, et al. (2004). "The DNA sequence and comparative analysis of human chromosome 10.". Nature 429 (6990): 375–81. doi:10.1038/nature02462. PMID 15164054.
Picard F, Kurtev M, Chung N, et al. (2004). "Sirt1 promotes fat mobilization in white adipocytes by repressing PPAR-gamma.". Nature 429 (6993): 771–6. doi:10.1038/nature02583. PMID 15175761.
Cohen HY, Miller C, Bitterman KJ, et al. (2004). "Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase.". Science 305 (5682): 390–2. doi:10.1126/science.1099196. PMID 15205477.