Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1

Biochemical and Biophysical Research Communications

Volumn 393, Issue 1, 2010, Pages 73-78

  Ogura, Masahito ^a   Nakamura, Yasuhiko ^a   Tanaka, Daisuke ^a   Zhuang, Xiaotong ^a   Fujita, Yoshihito ^a   Obara, Akio ^a   Hamasaki, Akihiro ^a   Hosokawa, Masaya ^a   Inagaki, Nobuya ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Liver; Mitochondria; SIRT5; Urea cycle

Indexed keywords

AMMONIA; CARBAMOYL PHOSPHATE SYNTHASE; MITOCHONDRIAL PROTEIN; SIRTUIN 5; UREA;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DEACETYLATION; DIET RESTRICTION; ELECTROPHORESIS; GENE OVEREXPRESSION; KNOCKOUT MOUSE; LIVER CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; TRANSGENIC MOUSE; UPREGULATION; WILD TYPE;

ACETYLATION; AMINO ACID SEQUENCE; AMMONIA; ANIMALS; CARBAMOYL-PHOSPHATE SYNTHASE (AMMONIA); ENZYME ACTIVATION; FASTING; HEPATOCYTES; MICE; MICE, KNOCKOUT; MICE, TRANSGENIC; MITOCHONDRIA, LIVER; MOLECULAR SEQUENCE DATA; PEPTIDES; RNA, MESSENGER; SIRTUINS; UP-REGULATION; UREA;

MAMMALIA; MUS;

EID: 77249128352     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.01.081     Document Type: Article

References (28)

1. Imai S., Armstrong C.M., Kaeberlein M., et al. Transcriptional silencing and longevity protein SIR2 is an NAD-dependent histone deacetylase. Nature 403 (2000) 795-800
2. Kaeberlein M., McVey M., and Guarente L. The SIR2/3/4 complex and SIR2 alone promote longevity in saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13 (1999) 2570-2580
3. Tissenbaum H.A., and Guarente L. Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410 (2001) 227-230
4. Rogina B., and Helfand S.L. SIR2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. USA 101 (2004) 15998-16003
5. Frye R.A. Phylogenetic classification of prokaryotic and eukaryotic SIR2-like proteins. Biochem. Biophys. Res. Commun. 273 (2000) 793-798
6. Rodgers J.T., Lerin C., Haas W., Gygi S.P., et al. Nutrient control of glucose homeostasis through a complex of PGC-1α and SIRT1. Nature 434 (2005) 113-118
7. Frescas D., Valent L., and Accili D. Nuclear trapping of the forkhead transcription factor FOXO1 via SIRT-dependent deacetylation promotes expression of glucogenetic genes. J. Biol. Chem. 280 (2005) 20589-20595
8. Nakamura Y., Ogura M., Tanaka D., et al. Localization of mouse mitochondrial SIRT proteins: shift of SIRT3 to nucleus by co-expression with SIRT5. Biochem. Biophys. Res. Commun. 366 1 (2008) 174-179
9. Hallows W.C., Lee S., and Denu J.M. Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases. Proc. Natl. Acad. Sci. USA 103 (2006) 10230-10235
10. Schwer B., Bunkenborg J., Verdin R.O., et al. Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl Acad. Sci. USA 103 (2005) 10224-10229
11. Schlicker C., Gertz M., Papatheodorou P., et al. Substrates and regulation mechanisms for the human mitochondrial sirtuins SIRT3 and SIRT5. J. Mol. Biol. 382 (2008) 790-801
12. Haigis M.C., Mostoslavsky R., Haigis K.M., et al. SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells. Cell 126 (2006) 941-954
13. +-dependent tubulin deacetylase. Mol. Cell. 11 (2003) 437-444
14. Nakagawa T., Lomb D.J., Haigis M., et al. SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle. Cell 137 (2009) 560-570
15. Jackson M.J., Beaudet A.L., and O'Brien W.E. Mammalian urea cycle enzymes. Annu. Rev. Genet. 20 (1986) 431-464
16. Deignan J.L., Cederbaum S.D., and Grody W.W. Contrasting features of urea cycle disorders in human patients and knockout mouse models. Mol. Genet. Metab. 93 (2008) 7-14
17. Miyazaki J., Araki K., Yamato E., et al. Establishment of a pancreatic beta cell line that retains glucose-inducible insulin secretion: special reference to expression of glucose transporter isoforms. Endocrinology 127 (1990) 126-132
18. Niwa H., Yamamua K., and Miyazaki J. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene 108 (1991) 193-200
19. Gupta S., Rogers L.K., Taylor S.K., et al. Inhibition of carbamyl phosphate synthetase-I and glutamine synthetase by hepatotoxic doses of acetaminophen in mice. Toxicol. Appl. Pharmacol. 146 (1997) 317-327
20. Fahien L.A., and Cohen P.P. A kinetic study of carbamyl phosphate synthetase. J. Biol. Chem. 239 (1964) 1925-1934
21. Hosokawa M., and Thorens B. Glucose release from GLUT2-null hepatocytes: characterization of a major and a minor pathway. Am. J. Physiol. Endocrinol. Metab. 282 (2002) E794-801
22. Cyr D.M., Egan S.G., Brini C.M., et al. On the mechanism of inhibition of gluconeogenesis and ureagenesis by sodium benzoate. Biochem. Pharmacol. 42 (1991) 645-654
23. Hunninghake D., and Grisolia S. A sensitive and convenient micromethod for estimation of urea, citrulline, and carbamyl derivatives. Anal. Biochem. 16 (1966) 200-205
24. Fearon W.R. The carbamido diacetyl reaction: a test for citrulline. Biochem. J. 33 (1939) 902-907
25. Nemoto S., Fergusson M.M., and Finkel T. Nutrient availability regulates SIRT1 through a forkhead-dependent pathway. Science 306 (2004) 2105-2108
26. Kim S.C., Sprung R., Chen Y., et al. Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol. Cell. 23 (2006) 607-618
27. Gomez M., Jorda A., Cabo J., et al. Effect of starvation on the N-acetylglutamate system of rat liver. FEBS. Lett. 156 (1983) 119-122
28. Tillman J.B., Dhahbi J.M., Mote P.L., et al. Dietary calorie restriction in mice induces carbamyl phosphate synthetase I gene transcription tissue specifically. J. Biol. Chem. 271 (1996) 3500-3506