메뉴 건너뛰기




Volumn 21, Issue 6, 2011, Pages 728-734

Understanding histone acetyltransferase Rtt109 structure and function: How many chaperones does it take?

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HISTONE ACETYLTRANSFERASE; HISTONE H3; PROTEIN ASF1; PROTEIN VPS75; REGULATOR OF TY1 TRANSPOSITION 109; UNCLASSIFIED DRUG;

EID: 82955203156     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2011.09.005     Document Type: Review
Times cited : (35)

References (31)
  • 2
    • 57049152851 scopus 로고    scopus 로고
    • Catalysis and substrate selection by histone/protein lysine acetyltransferases
    • Berndsen C.E., Denu J.M. Catalysis and substrate selection by histone/protein lysine acetyltransferases. Curr Opin Struct Biol 2008, 18:682-689.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 682-689
    • Berndsen, C.E.1    Denu, J.M.2
  • 3
    • 33846023720 scopus 로고    scopus 로고
    • Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II
    • Schneider J., Bajwa P., Johnson F.C., Bhaumik S.R., Shilatifard A. Rtt109 is required for proper H3K56 acetylation: a chromatin mark associated with the elongating RNA polymerase II. J Biol Chem 2006, 281:37270-37274.
    • (2006) J Biol Chem , vol.281 , pp. 37270-37274
    • Schneider, J.1    Bajwa, P.2    Johnson, F.C.3    Bhaumik, S.R.4    Shilatifard, A.5
  • 4
    • 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 2007, 315:649-652.
    • (2007) Science , vol.315 , pp. 649-652
    • Driscoll, R.1    Hudson, A.2    Jackson, S.P.3
  • 5
    • 33846796258 scopus 로고    scopus 로고
    • Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
    • Han J., Zhou H., Horazdovsky B., Zhang K., Xu R.M., Zhang Z. Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 2007, 315:653-655.
    • (2007) Science , vol.315 , pp. 653-655
    • Han, J.1    Zhou, H.2    Horazdovsky, B.3    Zhang, K.4    Xu, R.M.5    Zhang, Z.6
  • 7
    • 76849084692 scopus 로고    scopus 로고
    • A role for Gcn5 in replication-coupled nucleosome assembly
    • Burgess R.J., Zhou H., Han J., Zhang Z. A role for Gcn5 in replication-coupled nucleosome assembly. Mol Cell 2010, 37:469-480.
    • (2010) Mol Cell , vol.37 , pp. 469-480
    • Burgess, R.J.1    Zhou, H.2    Han, J.3    Zhang, Z.4
  • 9
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 1997, 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 11
    • 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 2005, 436:294-298.
    • (2005) Nature , vol.436 , pp. 294-298
    • Masumoto, H.1    Hawke, D.2    Kobayashi, R.3    Verreault, A.4
  • 12
    • 65549113750 scopus 로고    scopus 로고
    • CBP/p300-mediated acetylation of histone H3 on lysine 56
    • Das C., Lucia M.S., Hansen K.C., Tyler J.K. CBP/p300-mediated acetylation of histone H3 on lysine 56. Nature 2009, 459:113-117.
    • (2009) Nature , vol.459 , pp. 113-117
    • Das, C.1    Lucia, M.S.2    Hansen, K.C.3    Tyler, J.K.4
  • 13
    • 57049120143 scopus 로고    scopus 로고
    • Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function
    • Wang L., Tang Y., Cole P.A., Marmorstein R. Structure and chemistry of the p300/CBP and Rtt109 histone acetyltransferases: implications for histone acetyltransferase evolution and function. Curr Opin Struct Biol 2008, 18:741-747.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 741-747
    • Wang, L.1    Tang, Y.2    Cole, P.A.3    Marmorstein, R.4
  • 14
    • 79958773381 scopus 로고    scopus 로고
    • Interaction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo
    • Keck K.M., Pemberton L.F. Interaction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo. Traffic 2011.
    • (2011) Traffic
    • Keck, K.M.1    Pemberton, L.F.2
  • 15
  • 18
    • 80052247642 scopus 로고    scopus 로고
    • The activity of the histone chaperone yeast Asf1 in the assembly and disassembly of histone H3/H4-DNA complexes
    • Donham D.C., Scorgie J.K., Churchill M.E. The activity of the histone chaperone yeast Asf1 in the assembly and disassembly of histone H3/H4-DNA complexes. Nucleic Acids Res 2011, 39:5449-5458.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5449-5458
    • Donham, D.C.1    Scorgie, J.K.2    Churchill, M.E.3
  • 21
    • 77955033193 scopus 로고    scopus 로고
    • Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone complex
    • Albaugh B.N., Kolonko E.M., Denu J.M. Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone complex. Biochemistry 2010, 49:6375-6385.
    • (2010) Biochemistry , vol.49 , pp. 6375-6385
    • Albaugh, B.N.1    Kolonko, E.M.2    Denu, J.M.3
  • 23
    • 79960138904 scopus 로고    scopus 로고
    • Autoacetylation of the histone acetyltransferase RTT109
    • Albaugh B.N., Arnold K.M., Lee S., Denu J.M. Autoacetylation of the histone acetyltransferase RTT109. J Biol Chem 2011, 286:24694-24701.
    • (2011) J Biol Chem , vol.286 , pp. 24694-24701
    • Albaugh, B.N.1    Arnold, K.M.2    Lee, S.3    Denu, J.M.4
  • 24
    • 53049105934 scopus 로고    scopus 로고
    • Structural insights into histone H3 lysine 56 acetylation by Rtt109
    • Lin C., Yuan Y.A. Structural insights into histone H3 lysine 56 acetylation by Rtt109. Structure 2008, 16:1503-1510.
    • (2008) Structure , vol.16 , pp. 1503-1510
    • Lin, C.1    Yuan, Y.A.2
  • 25
    • 50449091106 scopus 로고    scopus 로고
    • Molecular basis for the autoregulation of the protein acetyl transferase Rtt109
    • Stavropoulos P., Nagy V., Blobel G., Hoelz A. Molecular basis for the autoregulation of the protein acetyl transferase Rtt109. Proc Natl Acad Sci USA 2008, 105:12236-12241.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 12236-12241
    • Stavropoulos, P.1    Nagy, V.2    Blobel, G.3    Hoelz, A.4
  • 27
    • 79955534838 scopus 로고    scopus 로고
    • Structure and histone binding properties of the vps75-rtt109 chaperone-lysine acetyltransferase complex
    • Su D., Hu Q., Zhou H., Thompson J.R., Xu R.M., Zhang Z., Mer G. Structure and histone binding properties of the vps75-rtt109 chaperone-lysine acetyltransferase complex. J Biol Chem 2011, 286:15625-15629.
    • (2011) J Biol Chem , vol.286 , pp. 15625-15629
    • Su, D.1    Hu, Q.2    Zhou, H.3    Thompson, J.R.4    Xu, R.M.5    Zhang, Z.6    Mer, G.7
  • 28
    • 50449106039 scopus 로고    scopus 로고
    • Structure of Vps75 and implications for histone chaperone function
    • Tang Y., Meeth K., Jiang E., Luo C., Marmorstein R. Structure of Vps75 and implications for histone chaperone function. Proc Natl Acad Sci USA 2008, 105:12206-12211.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 12206-12211
    • Tang, Y.1    Meeth, K.2    Jiang, E.3    Luo, C.4    Marmorstein, R.5
  • 30
    • 0036236469 scopus 로고    scopus 로고
    • Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro
    • Asahara H., Tartare-Deckert S., Nakagawa T., Ikehara T., Hirose F., Hunter T., Ito T., Montminy M. Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro. Mol Cell Biol 2002, 22:2974-2983.
    • (2002) Mol Cell Biol , vol.22 , pp. 2974-2983
    • Asahara, H.1    Tartare-Deckert, S.2    Nakagawa, T.3    Ikehara, T.4    Hirose, F.5    Hunter, T.6    Ito, T.7    Montminy, M.8
  • 31
    • 0033898468 scopus 로고    scopus 로고
    • P300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone
    • Ito T., Ikehara T., Nakagawa T., Kraus W.L., Muramatsu M. p300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone. Genes Dev 2000, 14:1899-1907.
    • (2000) Genes Dev , vol.14 , pp. 1899-1907
    • Ito, T.1    Ikehara, T.2    Nakagawa, T.3    Kraus, W.L.4    Muramatsu, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.