메뉴 건너뛰기




Volumn 12, Issue 3, 2010, Pages 294-298

Histone H3 Thr 45 phosphorylation is a replication-associated post-translational modification in S. cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; DNA; HISTONE H3; LYSINE; PROTEIN CDC7; PROTEIN DBF4; THREONINE; UNCLASSIFIED DRUG;

EID: 77649276054     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb2030     Document Type: Article
Times cited : (75)

References (33)
  • 1
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl, B. D. & Allis, C. D. The language of covalent histone modifications. Nature 403, 41-45 (2000).
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 2
    • 34347358721 scopus 로고    scopus 로고
    • Role of histone modification in chromatin dynamics
    • Ito, T. Role of histone modification in chromatin dynamics. J. Biochem. 141, 609-614 (2007).
    • (2007) J. Biochem. , vol.141 , pp. 609-614
    • Ito, T.1
  • 3
    • 22444448143 scopus 로고    scopus 로고
    • A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response
    • Masumoto, H., Hawke, D., Kobayashi, R. & Verreault, A. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 436, 294-298 (2005).
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 4
    • 33846796258 scopus 로고    scopus 로고
    • Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
    • Han, J. et al. Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315, 653-655 (2007).
    • (2007) Science , vol.315 , pp. 653-655
    • Han, J.1
  • 5
    • 0033289033 scopus 로고    scopus 로고
    • Identification and analysis of native nucleo-somal histone acetyltransferase complexes
    • Grant, P. A., Berger, S. L. & Workman, J. L. Identification and analysis of native nucleo-somal histone acetyltransferase complexes. Methods Mol. Biol. 119, 311-317 (1999).
    • (1999) Methods Mol. Biol. , vol.119 , pp. 311-317
    • Grant, P.A.1    Berger, S.L.2    Workman, J.L.3
  • 6
    • 0035839135 scopus 로고    scopus 로고
    • Snf1-a histone kinase that works in concert with the histone acetyl-transferase Gcn5 to regulate transcription
    • Lo, W. S. et al. Snf1-a histone kinase that works in concert with the histone acetyl-transferase Gcn5 to regulate transcription. Science 293, 1142-1146 (2001).
    • (2001) Science , vol.293 , pp. 1142-1146
    • Lo, W.S.1
  • 7
    • 0015796354 scopus 로고
    • Three additional genes required for deoxyribonucleic acid synthesis in Saccharomyces cerevisiae
    • Hartwell, L. H. Three additional genes required for deoxyribonucleic acid synthesis in Saccharomyces cerevisiae. J. Bacteriol. 115, 966-974 (1973).
    • (1973) J. Bacteriol. , vol.115 , pp. 966-974
    • Hartwell, L.H.1
  • 8
    • 0027192941 scopus 로고
    • Cell cycle regulation of the yeast Cdc7 protein kinase by association with the Dbf4 protein
    • Jackson, A. L., Pahl, P. M., Harrison, K., Rosamond, J. & Sclafani, R. A. Cell cycle regulation of the yeast Cdc7 protein kinase by association with the Dbf4 protein. Mol. Cell. Biol. 13, 2899-2908 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2899-2908
    • Jackson, A.L.1    Pahl, P.M.2    Harrison, K.3    Rosamond, J.4    Sclafani, R.A.5
  • 9
    • 0024545513 scopus 로고
    • The yeast gene, DBF4, essential for entry into S phase is cell cycle regulated
    • Chapman, J. W. & Johnston, L. H. The yeast gene, DBF4, essential for entry into S phase is cell cycle regulated. Exp. Cell Res. 180, 419-428 (1989).
    • (1989) Exp. Cell Res. , vol.180 , pp. 419-428
    • Chapman, J.W.1    Johnston, L.H.2
  • 10
    • 0033947670 scopus 로고    scopus 로고
    • Cdc7p-Dbf4p becomes famous in the cell cycle
    • Sclafani, R. A. Cdc7p-Dbf4p becomes famous in the cell cycle. J. Cell. Sci. 113 (Pt 12), 2111-2117 (2000).
    • (2000) J. Cell. Sci. , vol.113 , Issue.PART. 12 , pp. 2111-2117
    • Sclafani, R.A.1
  • 11
    • 0033215306 scopus 로고    scopus 로고
    • Cdc7p-Dbf4p kinase binds to chromatin during S phase and is regulated by both the APC and the RAD53 checkpoint pathway
    • Weinreich, M. & Stillman, B. Cdc7p-Dbf4p kinase binds to chromatin during S phase and is regulated by both the APC and the RAD53 checkpoint pathway. EMBO J. 18, 5334-5346 (1999).
    • (1999) EMBO J. , vol.18 , pp. 5334-5346
    • Weinreich, M.1    Stillman, B.2
  • 12
    • 0031435940 scopus 로고    scopus 로고
    • Mcm2 is a target of regulation by Cdc7-Dbf4 during the initiation of DNA synthesis
    • Lei, M. et al. Mcm2 is a target of regulation by Cdc7-Dbf4 during the initiation of DNA synthesis. Genes Dev. 11, 3365-3374 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 3365-3374
    • Lei, M.1
  • 13
    • 33845976373 scopus 로고    scopus 로고
    • Phosphorylation of MCM4 by Cdc7 kinase facilitates its interaction with Cdc45 on the chromatin
    • Masai, H. et al. Phosphorylation of MCM4 by Cdc7 kinase facilitates its interaction with Cdc45 on the chromatin. J. Biol. Chem. 281, 39249-39261 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 39249-39261
    • Masai, H.1
  • 14
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • White, C. L., Suto, R. K. & Luger, K. Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions. EMBO J. 20, 5207-5218 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5207-5218
    • White, C.L.1    Suto, R.K.2    Luger, K.3
  • 15
    • 33751241119 scopus 로고    scopus 로고
    • Histone H3 lysine 56 acetylation: A new twist in the chromosome cycle
    • Ozdemir, A., Masumoto, H., Fitzjohn, P., Verreault, A. & Logie, C. Histone H3 lysine 56 acetylation: a new twist in the chromosome cycle. Cell Cycle 5, 2602-2608 (2006).
    • (2006) Cell Cycle , vol.5 , pp. 2602-2608
    • Ozdemir, A.1    Masumoto, H.2    Fitzjohn, P.3    Verreault, A.4    Logie, C.5
  • 16
    • 34347363106 scopus 로고    scopus 로고
    • Histone tails and the H3 αn helix regulate nucleosome mobility and stability
    • Ferreira, H., Somers, J., Webster, R., Flaus, A. & Owen-Hughes, T. Histone tails and the H3 αN helix regulate nucleosome mobility and stability. Mol. Cell. Biol. 27, 4037-4048 (2007).
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4037-4048
    • Ferreira, H.1    Somers, J.2    Webster, R.3    Flaus, A.4    Owen-Hughes, T.5
  • 17
    • 22544441929 scopus 로고    scopus 로고
    • Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae
    • Ozdemir, A. et al. Characterization of lysine 56 of histone H3 as an acetylation site in Saccharomyces cerevisiae. J. Biol. Chem. 280, 25949-25952 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 25949-25952
    • Ozdemir, A.1
  • 18
    • 33846818840 scopus 로고    scopus 로고
    • Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56
    • Driscoll, R., Hudson, A. & Jackson, S. P. Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56. Science 315, 649-652 (2007).
    • (2007) Science , vol.315 , pp. 649-652
    • Driscoll, R.1    Hudson, A.2    Jackson, S.P.3
  • 20
    • 0344413644 scopus 로고    scopus 로고
    • Cdc7 kinases (DDKs) and checkpoint responses: Lessons from two yeasts
    • Duncker, B. P. & Brown, G. W. Cdc7 kinases (DDKs) and checkpoint responses: lessons from two yeasts. Mutat. Res. 532, 21-27 (2003).
    • (2003) Mutat. Res. , vol.532 , pp. 21-27
    • Duncker, B.P.1    Brown, G.W.2
  • 21
    • 57749116059 scopus 로고    scopus 로고
    • The role of Dbf4/Drf1-dependent kinase Cdc7 in DNA-damage checkpoint control
    • Tsuji, T., Lau, E., Chiang, G. G. & Jiang, W. The role of Dbf4/Drf1-dependent kinase Cdc7 in DNA-damage checkpoint control. Mol. Cell 32, 862-869 (2008).
    • (2008) Mol. Cell , vol.32 , pp. 862-869
    • Tsuji, T.1    Lau, E.2    Chiang, G.G.3    Jiang, W.4
  • 22
    • 67650215370 scopus 로고    scopus 로고
    • Phosphorylation of histone H3 Thr-45 is linked to apoptosis
    • Hurd, P. J. et al. Phosphorylation of histone H3 Thr-45 is linked to apoptosis. J. Biol. Chem. 284, 16575-16583 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 16575-16583
    • Hurd, P.J.1
  • 23
    • 1642326716 scopus 로고    scopus 로고
    • Phosphorylation of histone H3: A balancing act between chromosome condensation and transcriptional activation
    • Nowak, S. J. & Corces V. G. Phosphorylation of histone H3: a balancing act between chromosome condensation and transcriptional activation. Trends Genet. 20, 214-220 (2004).
    • (2004) Trends Genet. , vol.20 , pp. 214-220
    • Nowak, S.J.1    Corces, V.G.2
  • 24
    • 11844276610 scopus 로고    scopus 로고
    • Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen peroxide-induced apoptosis in S. cerevisiae
    • Ahn, S. H. et al. Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen peroxide-induced apoptosis in S. cerevisiae. Cell 120, 25-36 (2005).
    • (2005) Cell , vol.120 , pp. 25-36
    • Ahn, S.H.1
  • 25
    • 0033291650 scopus 로고    scopus 로고
    • Analysis of nucleosome disruption by ATP-driven chromatin remodeling complexes
    • Owen-Hughes, T. et al. Analysis of nucleosome disruption by ATP-driven chromatin remodeling complexes. Methods Mol. Biol. 119, 319-331 (1999).
    • (1999) Methods Mol. Biol. , vol.119 , pp. 319-331
    • Owen-Hughes, T.1
  • 26
    • 0033289033 scopus 로고    scopus 로고
    • Identification and analysis of native nucleosomal histone acetyltransferase complexes
    • Grant, P. A., Berger, S. L. & Workman, J. L. Identification and analysis of native nucleosomal histone acetyltransferase complexes. Methods Mol. Biol. 119, 311-317 (1999).
    • (1999) Methods Mol. Biol. , vol.119 , pp. 311-317
    • Grant, P.A.1    Berger, S.L.2    Workman, J.L.3
  • 27
    • 31444445458 scopus 로고    scopus 로고
    • A phosphatase complex that dephosphorylates γh2AX regulates DNA damage checkpoint recovery
    • Keogh, M. C. et al. A phosphatase complex that dephosphorylates γH2AX regulates DNA damage checkpoint recovery. Nature 439, 497-501 (2006).
    • (2006) Nature , vol.439 , pp. 497-501
    • Keogh, M.C.1
  • 28
    • 85078505418 scopus 로고    scopus 로고
    • Improved flow cytometric analysis of the budding yeast cell cycle
    • Haase, S. B. & Reed, S. I. Improved flow cytometric analysis of the budding yeast cell cycle. Cell Cycle 1, 132-136 (2002).
    • (2002) Cell Cycle , vol.1 , pp. 132-136
    • Haase, S.B.1    Reed, S.I.2
  • 29
    • 0025093599 scopus 로고
    • Genetic analysis of histone H4: Essential role of lysines subject to reversible acetylation
    • Megee, P. C., Morgan, B. A., Mittman, B. A. & Smith, M. M. Genetic analysis of histone H4: essential role of lysines subject to reversible acetylation. Science 247, 841-845 (1990).
    • (1990) Science , vol.247 , pp. 841-845
    • Megee, P.C.1    Morgan, B.A.2    Mittman, B.A.3    Smith, M.M.4
  • 30
    • 0017527790 scopus 로고
    • Cell cycle of Saccharomyces cerevisiae in populations growing at different rates
    • Slater, M. L., Sharrow, S. O. & Gart, J. J. Cell cycle of Saccharomyces cerevisiae in populations growing at different rates. Proc Natl Acad Sci USA 74, 3850-3854 (1977).
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 3850-3854
    • Slater, M.L.1    Sharrow, S.O.2    Gart, J.J.3
  • 31
    • 0030797349 scopus 로고    scopus 로고
    • Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: Characterization of an Ada complex and the SAGA (Spt/Ada) complex
    • Grant, P. A. et al. Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex. Genes Dev. 11, 1640-1650 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 1640-1650
    • Grant, P.A.1
  • 32
    • 13444267442 scopus 로고    scopus 로고
    • Chd1 chromodomain links histone H3 methylation with SAGA-and SLIK-dependent acetyla-tion
    • Pray-Grant, M. G., Daniel, J. A., Schieltz, D., Yates, J. R., 3rd & Grant, P. A. Chd1 chromodomain links histone H3 methylation with SAGA-and SLIK-dependent acetyla-tion. Nature 433, 434-438 (2005).
    • (2005) Nature , vol.433 , pp. 434-438
    • Pray-Grant, M.G.1    Daniel, J.A.2    Schieltz, D.3    Yates III, J.R.4    Grant, P.A.5
  • 33
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut, G. et al. A generic protein purification method for protein complex characterization and proteome exploration. Nature Biotechnol. 17, 1030-1032 (1999).
    • (1999) Nature Biotechnol. , vol.17 , pp. 1030-1032
    • Rigaut, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.