메뉴 건너뛰기




Volumn 20, Issue 1, 2011, Pages 131-139

Structure of Sir2Tm bound to a propionylated peptide

Author keywords

Deacetylation; Depropionylation; Propionyl lysine; Sir2; Sirtuin; T. maritima

Indexed keywords

LYSINE; PEPTIDE; SIRTUIN 2;

EID: 78650786849     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.544     Document Type: Article
Times cited : (19)

References (42)
  • 1
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • Starai VJ, Celic I, Cole RN, Boeke JD, Escalante-Semerena JC (2002) Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 298:2390-2392.
    • (2002) Science , vol.298 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 5
    • 0035895275 scopus 로고    scopus 로고
    • Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: Evidence for acetyl transfer from substrate to an NAD breakdown product
    • Tanny JC, Moazed D (2001) Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: evidence for acetyl transfer from substrate to an NAD breakdown product. Proc Natl Acad Sci USA 98:415-420.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 415-420
    • Tanny, J.C.1    Moazed, D.2
  • 7
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai S, Armstrong CM, Kaeberlein M, Guarente L (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403:795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 10
    • 0037291214 scopus 로고    scopus 로고
    • The human Sir2 ortholog, SIRT2, is an NAD+dependent tubulin deacetylase
    • North BJ, Marshall BL, Borra MT, Denu JM, Verdin E (2003) The human Sir2 ortholog, SIRT2, is an NAD+dependent tubulin deacetylase. Mol Cell 11:437-444.
    • (2003) Mol Cell , vol.11 , pp. 437-444
    • North, B.J.1    Marshall, B.L.2    Borra, M.T.3    Denu, J.M.4    Verdin, E.5
  • 11
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability
    • Brachmann CB, Sherman JM, Devine SE, Cameron EE, Pillus L, Boeke JD (1995) The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability. Genes Dev 9:2888-2902.
    • (1995) Genes Dev , vol.9 , pp. 2888-2902
    • Brachmann, C.B.1    Sherman, J.M.2    Devine, S.E.3    Cameron, E.E.4    Pillus, L.5    Boeke, J.D.6
  • 12
    • 0024536650 scopus 로고
    • A new role for a yeast transcriptional silencer gene, SIR2, in regulation of recombination in ribosomal DNA
    • Gottlieb S, Esposito RE (1989) A new role for a yeast transcriptional silencer gene, SIR2, in regulation of recombination in ribosomal DNA. Cell 56:771-776.
    • (1989) Cell , vol.56 , pp. 771-776
    • Gottlieb, S.1    Esposito, R.E.2
  • 13
    • 0031056907 scopus 로고    scopus 로고
    • An unusual form of transcriptional silencing in yeast ribosomal DNA
    • Smith JS, Boeke JD (1997) An unusual form of transcriptional silencing in yeast ribosomal DNA. Genes Dev 11:241-254.
    • (1997) Genes Dev , vol.11 , pp. 241-254
    • Smith, J.S.1    Boeke, J.D.2
  • 15
    • 0035917536 scopus 로고    scopus 로고
    • Crystal structure of a SIR2 homolog-NAD complex
    • Min J, Landry J, Sternglanz R, Xu RM (2001) Crystal structure of a SIR2 homolog-NAD complex. Cell 105: 269-279.
    • (2001) Cell , vol.105 , pp. 269-279
    • Min, J.1    Landry, J.2    Sternglanz, R.3    Xu, R.M.4
  • 18
    • 0242626891 scopus 로고    scopus 로고
    • Structure of the yeast Hst2 protein deacetylase in ternary complex with 20-O-acetyl ADP ribose and histone peptide
    • Zhao K, Chai X, Marmorstein R (2003) Structure of the yeast Hst2 protein deacetylase in ternary complex with 20-O-acetyl ADP ribose and histone peptide. Structure 11:1403-1411.
    • (2003) Structure , vol.11 , pp. 1403-1411
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 19
    • 1542298916 scopus 로고    scopus 로고
    • Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli
    • Zhao K, Chai X, Marmorstein R (2004) Structure and substrate binding properties of cobB, a Sir2 homolog protein deacetylase from Escherichia coli. J Mol Biol 337:731-741.
    • (2004) J Mol Biol , vol.337 , pp. 731-741
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3
  • 22
    • 0033600176 scopus 로고    scopus 로고
    • 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
    • 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 260:273-279.
    • (1999) Biochem Biophys Res Commun , vol.260 , pp. 273-279
    • Frye, R.A.1
  • 23
    • 0033610894 scopus 로고    scopus 로고
    • CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2
    • Tsang AW, Escalante-Semerena JC (1998) CobB, a new member of the SIR2 family of eucaryotic regulatory proteins, is required to compensate for the lack of nicotinate mononucleotide: 5,6-dimethylbenzimidazole phosphoribosyltransferase activity in cobT mutants during cobalamin biosynthesis in Salmonella typhimurium LT2. J Biol Chem 273:31788-31794.
    • (1998) J Biol Chem , vol.273 , pp. 31788-31794
    • Tsang, A.W.1    Escalante-Semerena, J.C.2
  • 24
    • 0033598942 scopus 로고    scopus 로고
    • An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing
    • Tanny JC, Dowd GJ, Huang J, Hilz H, Moazed D (1999) An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing. Cell 99:735-745.
    • (1999) Cell , vol.99 , pp. 735-745
    • Tanny, J.C.1    Dowd, G.J.2    Huang, J.3    Hilz, H.4    Moazed, D.5
  • 25
    • 37549067781 scopus 로고    scopus 로고
    • Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases
    • Smith BC, Denu JM (2007) Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases J Biol Chem 282:37256-37265.
    • (2007) J Biol Chem , vol.282 , pp. 37256-37265
    • Smith, B.C.1    Denu, J.M.2
  • 26
    • 34248595983 scopus 로고    scopus 로고
    • Sir2 deacetylases exhibit nucleophilic participation of acetyl-lysine in NAD+ cleavage
    • Smith BC, Denu JM (2007) Sir2 deacetylases exhibit nucleophilic participation of acetyl-lysine in NAD+ cleavage. J Am Chem Soc 129:5802-5803.
    • (2007) J Am Chem Soc , vol.129 , pp. 5802-5803
    • Smith, B.C.1    Denu, J.M.2
  • 27
    • 33745534953 scopus 로고    scopus 로고
    • Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide
    • Hoff KG, Avalos JL, Sens K, Wolberger C (2006) Insights into the sirtuin mechanism from ternary complexes containing NAD+ and acetylated peptide. Structure 14:1231-1240.
    • (2006) Structure , vol.14 , pp. 1231-1240
    • Hoff, K.G.1    Avalos, J.L.2    Sens, K.3    Wolberger, C.4
  • 29
    • 0001396232 scopus 로고    scopus 로고
    • On the meaning of Km and V/K in enzyme kinetics
    • Northrop DB (1998) On the Meaning of Km and V/K in Enzyme Kinetics. J Chem Educ 75:1153-1157.
    • (1998) J Chem Educ , vol.75 , pp. 1153-1157
    • Northrop, D.B.1
  • 30
    • 0016734139 scopus 로고
    • Partition analysis and the concept of net rate constants as tools in enzyme kinetics
    • Cleland WW (1975) Partition analysis and the concept of net rate constants as tools in enzyme kinetics. Biochemistry 14:3220-3224.
    • (1975) Biochemistry , vol.14 , pp. 3220-3224
    • Cleland, W.W.1
  • 31
    • 0346435109 scopus 로고    scopus 로고
    • Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases
    • Jackson MD, Schmidt MT, Oppenheimer NJ, Denu JM (2003) Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. J Biol Chem 278:50985-50998.
    • (2003) J Biol Chem , vol.278 , pp. 50985-50998
    • Jackson, M.D.1    Schmidt, M.T.2    Oppenheimer, N.J.3    Denu, J.M.4
  • 32
    • 3343024449 scopus 로고    scopus 로고
    • Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases
    • Borra MT, Langer MR, Slama JT, Denu JM (2004) Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases. Biochemistry 43:9877-9887.
    • (2004) Biochemistry , vol.43 , pp. 9877-9887
    • Borra, M.T.1    Langer, M.R.2    Slama, J.T.3    Denu, J.M.4
  • 33
    • 0041571570 scopus 로고    scopus 로고
    • Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry
    • Sauve AA, Schramm VL (2003) Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry. Biochemistry 42:9249-9256.
    • (2003) Biochemistry , vol.42 , pp. 9249-9256
    • Sauve, A.A.1    Schramm, V.L.2
  • 35
    • 0000351816 scopus 로고
    • What limits the rate of an enzymecatalyzed reaction?
    • Cleland WW (1975) What limits the rate of an enzymecatalyzed reaction? Acc Chem Res 8:145-151.
    • (1975) Acc Chem Res , vol.8 , pp. 145-151
    • Cleland, W.W.1
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
  • 39
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 40
    • 0003845223 scopus 로고    scopus 로고
    • Palo Alto, California:DeLano Scientific; Available at
    • Delano WL (2008) The PyMOL molecular graphics system. Palo Alto, California:DeLano Scientific; Available at: http://www.pymol.org.
    • (2008) The PyMOL Molecular Graphics System
    • Delano, W.L.1
  • 42
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger AT (2007) Version 1.2 of the Crystallography and NMR System. Nature Protocols 2:2728-2733.
    • (2007) Nature Protocols , vol.2 , pp. 2728-2733
    • Brunger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.