메뉴 건너뛰기




Volumn 415, Issue 3, 2008, Pages 377-386

The Leishmania infantum cytosolic SIR2-related protein 1 (LiSIR2RP1) is an NAD+-dependent deacetylase and ADP-ribosyltransferase

Author keywords

tubulin; ADP ribosyltransferase; Cytoskeleton; Leishmania infantum SIR2 related protein 1 (LiSIR2RP1); NAD+ dependent deacetylase; Parasite

Indexed keywords

ADP-RIBOSYLTRANSFERASE; CYTOSKELETON; LEISHMANIA INFANTUM SIR2-RELATED PROTEIN 1 (LISIR2RP1); NAD+ -DEPENDENT DEACETYLASE; PARASITE;

EID: 58149157691     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20080666     Document Type: Article
Times cited : (33)

References (52)
  • 1
    • 0028841317 scopus 로고
    • The SIR2 gene family, conserved from bacteria to humans, functions in silencing, cell cycle progression, and chromosome stability
    • Brachmann, C. B., Sherman, J. M., Devine, S. E., Cameron, E. E., Pillus, L. and Boeke, J. D. (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
  • 3
    • 0031056907 scopus 로고    scopus 로고
    • An unusual form of transcriptional silencing in yeast ribosomal DNA
    • Smith, J. S. and Boeke, J. D. (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
  • 4
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S., Armstrong, C. M., Kaeberlein, M. and 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
  • 5
    • 3943054839 scopus 로고    scopus 로고
    • The Sir2 family of protein deacetylases
    • Blander, G. and Guarente,. (2004) The Sir2 family of protein deacetylases. Annu. Rev. Biochem. 73, 417-435
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 417-435
    • Blander, G.1    Guarente2
  • 6
    • 0032098328 scopus 로고    scopus 로고
    • Leishmania major: Cell type dependent distribution of a 43kDa antigen related to silent information regulatory-2 protein family
    • Zemzoumi, K., Sereno, D., Francois, C., Guilvard, E., Lemesre, J. L. and Ouaissi, A. (1998) Leishmania major: cell type dependent distribution of a 43kDa antigen related to silent information regulatory-2 protein family. Biol. Cell 90, 239-245
    • (1998) Biol. Cell , vol.90 , pp. 239-245
    • Zemzoumi, K.1    Sereno, D.2    Francois, C.3    Guilvard, E.4    Lemesre, J.L.5    Ouaissi, A.6
  • 7
    • 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, R. A. (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
  • 8
    • 0033887456 scopus 로고    scopus 로고
    • Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins
    • Frye, R. A. (2000) Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins. Biochem. Biophys. Res. Commun. 273, 793-798
    • (2000) Biochem. Biophys. Res. Commun , vol.273 , pp. 793-798
    • Frye, R.A.1
  • 12
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2α promotes cell survival under stress
    • Luo, J., Nikolaev, A. Y., Imai, S., Chen, D., Su, F., Shiloh, A., Guarente, L. and Gu, W. (2001) Negative control of p53 by Sir2α promotes cell survival under stress. Cell 107, 137-148
    • (2001) Cell , vol.107 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 13
    • 0035868764 scopus 로고    scopus 로고
    • Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription
    • Muth, V., Nadaud, S., Grummt, I. and Voit, R. (2001) Acetylation of TAF(I)68, a subunit of TIF-IB/SL1, activates RNA polymerase I transcription. EMBO J. 20, 1353-1362
    • (2001) EMBO J , vol.20 , pp. 1353-1362
    • Muth, V.1    Nadaud, S.2    Grummt, I.3    Voit, R.4
  • 16
    • 0037405043 scopus 로고    scopus 로고
    • Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle
    • Dryden, S. C., Nahhas, F. A., Nowak, J. E., Goustin, A. S. and Tainsky, M. A. (2003) Role for human SIRT2 NAD-dependent deacetylase activity in control of mitotic exit in the cell cycle. Mol. Cell. Biol. 23, 3173-3185
    • (2003) Mol. Cell. Biol , vol.23 , pp. 3173-3185
    • Dryden, S.C.1    Nahhas, F.A.2    Nowak, J.E.3    Goustin, A.S.4    Tainsky, M.A.5
  • 18
    • 33745889628 scopus 로고    scopus 로고
    • Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2
    • Schwer, B., Bunkenborg, J., Verdin, R. O., Andersen, J. S. and Verdin, E. (2006) Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. Proc. Natl. Acad. Sci. U.S.A. 103, 10224-10229
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 10224-10229
    • Schwer, B.1    Bunkenborg, J.2    Verdin, R.O.3    Andersen, J.S.4    Verdin, E.5
  • 19
    • 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, J. C. and 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. U.S.A. 98, 415-420
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 415-420
    • Tanny, J.C.1    Moazed, D.2
  • 21
    • 0033598942 scopus 로고    scopus 로고
    • An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing
    • Tanny, J. C., Dowd, G. J., Huang, J., Hilz, H. and 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
  • 22
    • 0242556798 scopus 로고    scopus 로고
    • A chromosomal SIR2 homologue with both histone NAD-dependent ADP-ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei
    • Garcia-Salcedo, J. A., Gijon, P., Nolan, D. P., Tebabi, P. and Pays, E. (2003) A chromosomal SIR2 homologue with both histone NAD-dependent ADP-ribosyltransferase and deacetylase activities is involved in DNA repair in Trypanosoma brucei. EMBO J. 22, 5851-5862
    • (2003) EMBO J , vol.22 , pp. 5851-5862
    • Garcia-Salcedo, J.A.1    Gijon, P.2    Nolan, D.P.3    Tebabi, P.4    Pays, E.5
  • 23
    • 20444409132 scopus 로고    scopus 로고
    • Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase
    • Liszt, G., Ford, E., Kurtev, M. and Guarente, L. (2005) Mouse Sir2 homolog SIRT6 is a nuclear ADP-ribosyltransferase. J. Biol. Chem. 280, 21313-21320
    • (2005) J. Biol. Chem , vol.280 , pp. 21313-21320
    • Liszt, G.1    Ford, E.2    Kurtev, M.3    Guarente, L.4
  • 24
    • 36849009695 scopus 로고    scopus 로고
    • Plasmodium falciparum Sir2: An unusual sirtuin with dual histone deacetylase and ADP-ribosyltransferase activity
    • Merrick, C. J. and Duraisingh, MT. (2007) Plasmodium falciparum Sir2: an unusual sirtuin with dual histone deacetylase and ADP-ribosyltransferase activity. Eukaryot. Cell 6, 2081-2091
    • (2007) Eukaryot. Cell , vol.6 , pp. 2081-2091
    • Merrick, C.J.1    Duraisingh, M.T.2
  • 25
    • 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, A. W. and Escalante-Semerena, J. C. (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
  • 26
    • 0035826271 scopus 로고    scopus 로고
    • Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans
    • Tissenbaum, H. A. and Guarente, L. (2001) Increased dosage of a sir-2 gene extends lifespan in Caenorhabditis elegans. Nature 410, 227-230
    • (2001) Nature , vol.410 , pp. 227-230
    • Tissenbaum, H.A.1    Guarente, L.2
  • 27
    • 0033214237 scopus 로고    scopus 로고
    • The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms
    • Kaeberlein, M., McVey, M. and Guarente, L. (1999) The SIR2/3/4 complex and SIR2 alone promote longevity in Saccharomyces cerevisiae by two different mechanisms. Genes Dev. 13, 2570-2580
    • (1999) Genes Dev , vol.13 , pp. 2570-2580
    • Kaeberlein, M.1    McVey, M.2    Guarente, L.3
  • 28
    • 8644224064 scopus 로고    scopus 로고
    • Sir2 mediates longevity in the fly through a pathway related to calorie restriction
    • Rogina, B. and Helfand, S. L. (2004) Sir2 mediates longevity in the fly through a pathway related to calorie restriction. Proc. Natl. Acad. Sci. U.S.A. 101, 15998-15003
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 15998-15003
    • Rogina, B.1    Helfand, S.L.2
  • 29
    • 0037151779 scopus 로고    scopus 로고
    • Cytoplasmic SIR2 homologue overexpression promotes survival of Leishmania parasites by preventing programmed cell death
    • Vergnes, B., Sereno, D., Madjidian-Sereno, N., Lemesre, J. L. and Ouaissi, A. (2002) Cytoplasmic SIR2 homologue overexpression promotes survival of Leishmania parasites by preventing programmed cell death. Gene 296, 139-150
    • (2002) Gene , vol.296 , pp. 139-150
    • Vergnes, B.1    Sereno, D.2    Madjidian-Sereno, N.3    Lemesre, J.L.4    Ouaissi, A.5
  • 32
    • 0023110716 scopus 로고
    • Subpellicular and flagellar microtubules of Trypanosoma brucei brucei contain the same α tubulin isoforms
    • Schneider, A., Sherwin, T., Russell, D. G., Gull, K. and Seebeck, T. (1987) Subpellicular and flagellar microtubules of Trypanosoma brucei brucei contain the same α tubulin isoforms. J. Cell Biol. 104, 431-438
    • (1987) J. Cell Biol , vol.104 , pp. 431-438
    • Schneider, A.1    Sherwin, T.2    Russell, D.G.3    Gull, K.4    Seebeck, T.5
  • 33
    • 0026567861 scopus 로고
    • Microtubule protein ADP-ribosylation in vitro leads to assembly inhibition and rapid depolymerization
    • Scaife, R. M., Wilson, L. and Purich, D. L. (1992) Microtubule protein ADP-ribosylation in vitro leads to assembly inhibition and rapid depolymerization. Biochemistry 31, 310-316
    • (1992) Biochemistry , vol.31 , pp. 310-316
    • Scaife, R.M.1    Wilson, L.2    Purich, D.L.3
  • 35
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: A regulatory modification to rival phosphorylation?
    • Kouzarides, T. (2000) Acetylation: a regulatory modification to rival phosphorylation? EMBO J. 19, 1176-1179
    • (2000) EMBO J , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 36
    • 37349064941 scopus 로고    scopus 로고
    • An essential role for the Leishmania major metacaspase in cell cycle progression
    • Ambit, A., Fasel, N., Coombs, G. H. and Mottram, J. C. (2008) An essential role for the Leishmania major metacaspase in cell cycle progression. Cell Death Differ. 15, 113-122
    • (2008) Cell Death Differ , vol.15 , pp. 113-122
    • Ambit, A.1    Fasel, N.2    Coombs, G.H.3    Mottram, J.C.4
  • 37
    • 0034903608 scopus 로고    scopus 로고
    • A developmentally regulated rab11 homologue in Trypanosoma brucei is involved in recycling processes
    • Jeffries, T. R., Morgan, G. W. and Field, M. C. (2001) A developmentally regulated rab11 homologue in Trypanosoma brucei is involved in recycling processes. J. Cell Sci. 114, 2617-2626
    • (2001) J. Cell Sci , vol.114 , pp. 2617-2626
    • Jeffries, T.R.1    Morgan, G.W.2    Field, M.C.3
  • 38
    • 0025128705 scopus 로고
    • Purification and assembly in vitro of tubulin from Trypanosoma brucei
    • MacRae, T. H. and Gull, K. (1990) Purification and assembly in vitro of tubulin from Trypanosoma brucei. Biochem. J. 265, 87-93
    • (1990) Biochem. J , vol.265 , pp. 87-93
    • MacRae, T.H.1    Gull, K.2
  • 39
    • 0014755202 scopus 로고
    • Spindle microtubules in the dividing nuclei of trypanosomes
    • Vickerman, K. and Preston, T. M. (1970) Spindle microtubules in the dividing nuclei of trypanosomes. J. Cell Sci. 6, 365-383
    • (1970) J. Cell Sci , vol.6 , pp. 365-383
    • Vickerman, K.1    Preston, T.M.2
  • 41
    • 0034597639 scopus 로고    scopus 로고
    • Cytoskeleton: Functions for tubulin modifications at last
    • Rosenbaum, J. (2000) Cytoskeleton: functions for tubulin modifications at last. Curr. Biol. 10, 801-803
    • (2000) Curr. Biol , vol.10 , pp. 801-803
    • Rosenbaum, J.1
  • 43
    • 41949129135 scopus 로고    scopus 로고
    • Acetylation-dependent ADP-ribosylation by Trypanosoma brucei Sir2
    • Kowieski, T. M., Lee, S. and Denu, J. M. (2008) Acetylation-dependent ADP-ribosylation by Trypanosoma brucei Sir2. J. Biol. Chem. 283, 5317-5326
    • (2008) J. Biol. Chem , vol.283 , pp. 5317-5326
    • Kowieski, T.M.1    Lee, S.2    Denu, J.M.3
  • 44
    • 0034214285 scopus 로고    scopus 로고
    • Locus specificity determinants in the multifunctional yeast silencing protein Sir2
    • Cuperus, G., Shafaatian, R. and Shore, D. (2000) Locus specificity determinants in the multifunctional yeast silencing protein Sir2. EMBO J. 19, 2641-2651
    • (2000) EMBO J , vol.19 , pp. 2641-2651
    • Cuperus, G.1    Shafaatian, R.2    Shore, D.3
  • 45
    • 0033045090 scopus 로고    scopus 로고
    • Regional regulation of microtubule dynamics in polarized, motile cells
    • Wadsworth, P. (1999) Regional regulation of microtubule dynamics in polarized, motile cells. Cell Motil. Cytoskeleton 42, 48-59
    • (1999) Cell Motil. Cytoskeleton , vol.42 , pp. 48-59
    • Wadsworth, P.1
  • 46
    • 0037448671 scopus 로고    scopus 로고
    • Cell biology: Tubulin acetylation and cell motility
    • Palazzo, A., Ackerman, B. and Gundersen, G. G. (2003) Cell biology: tubulin acetylation and cell motility. Nature 16, 230
    • (2003) Nature , vol.16 , pp. 230
    • Palazzo, A.1    Ackerman, B.2    Gundersen, G.G.3
  • 47
    • 0029035184 scopus 로고
    • Acetylation of lysine 40 in α-tubulin is not essential in Tetrahymena thermophila
    • Gaertig, J., Cruz, M. A., Bowen, J., Gu, L., Pennock, D. G. and Gorovsky, M. A. (1995) Acetylation of lysine 40 in α-tubulin is not essential in Tetrahymena thermophila. J. Cell Biol. 129, 1301-1310
    • (1995) J. Cell Biol , vol.129 , pp. 1301-1310
    • Gaertig, J.1    Cruz, M.A.2    Bowen, J.3    Gu, L.4    Pennock, D.G.5    Gorovsky, M.A.6
  • 52
    • 0036591962 scopus 로고    scopus 로고
    • Biogenesis of Leishmania-harbouring parasitophorous vacuoles following phagocytosis of the metacyclic promastigote or amastigote stages of the parasites
    • Courret, N., Frehel, C., Gouhier, N., Pouchelet, M., Prina, E., Roux, P. and Antoine, J. C. (2002) Biogenesis of Leishmania-harbouring parasitophorous vacuoles following phagocytosis of the metacyclic promastigote or amastigote stages of the parasites. J. Cell Sci. 111, 2303-2316
    • (2002) J. Cell Sci , vol.111 , pp. 2303-2316
    • Courret, N.1    Frehel, C.2    Gouhier, N.3    Pouchelet, M.4    Prina, E.5    Roux, P.6    Antoine, J.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.