메뉴 건너뛰기




Volumn 30, Issue 10, 2016, Pages 1198-1210

The enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition

Author keywords

Cell cycle progression; Chromatin; Histone acetyltransferase; PCNA unloading

Indexed keywords

CYCLINE; HISTONE ACETYLTRANSFERASE; PROTEIN DERIVATIVE; PROTEIN ELG1; PROTEIN ENOK; UNCLASSIFIED DRUG; CHROMATIN; DROSOPHILA PROTEIN; ELG1 PROTEIN, DROSOPHILA; ENOK PROTEIN, DROSOPHILA; PROTEIN BINDING; PROTEIN SUBUNIT;

EID: 84969793635     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.271429.115     Document Type: Article
Times cited : (14)

References (43)
  • 1
    • 0041966011 scopus 로고    scopus 로고
    • Elg1 forms an alternative RFC complex important for DNA replication and genome integrity
    • Bellaoui M, Chang M, Ou J, Xu H, Boone C, Brown GW. 2003. Elg1 forms an alternative RFC complex important for DNA replication and genome integrity. EMBO J 22: 4304-4313.
    • (2003) EMBO J , vol.22 , pp. 4304-4313
    • Bellaoui, M.1    Chang, M.2    Ou, J.3    Xu, H.4    Boone, C.5    Brown, G.W.6
  • 2
    • 0042191693 scopus 로고    scopus 로고
    • ELG1, a yeast gene required for genome stability, forms a complex related to replication factor C
    • Ben-Aroya S, Koren A, Liefshitz B, Steinlauf R, Kupiec M. 2003. ELG1, a yeast gene required for genome stability, forms a complex related to replication factor C. Proc Natl Acad Sci 100: 9906-9911.
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 9906-9911
    • Ben-Aroya, S.1    Koren, A.2    Liefshitz, B.3    Steinlauf, R.4    Kupiec, M.5
  • 3
    • 1342268256 scopus 로고    scopus 로고
    • Fluorescent BrdU labeling and nuclear flow sorting of the Drosophila ovary
    • Calvi BR, Lilly MA. 2004. Fluorescent BrdU labeling and nuclear flow sorting of the Drosophila ovary. Methods Mol Biol 247: 203-213.
    • (2004) Methods Mol Biol , vol.247 , pp. 203-213
    • Calvi, B.R.1    Lilly, M.A.2
  • 4
    • 29544444195 scopus 로고    scopus 로고
    • ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation
    • Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J. 2006. ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation. Mol Cell 21: 51-64.
    • (2006) Mol Cell , vol.21 , pp. 51-64
    • Doyon, Y.1    Cayrou, C.2    Ullah, M.3    Landry, A.J.4    Cote, V.5    Selleck, W.6    Lane, W.S.7    Tan, S.8    Yang, X.J.9    Cote, J.10
  • 5
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JR. 1994. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. JAmSoc Mass Spectrom 5: 976-989.
    • (1994) Jamsoc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 6
    • 33746500659 scopus 로고    scopus 로고
    • Proteomic analysis by multidimensional protein identification technology
    • Florens L, Washburn MP. 2006. Proteomic analysis by multidimensional protein identification technology. Methods Mol Biol 328: 159-175.
    • (2006) Methods Mol Biol , vol.328 , pp. 159-175
    • Florens, L.1    Washburn, M.P.2
  • 7
    • 8644285427 scopus 로고    scopus 로고
    • Idling by DNA polymerase δ maintains a ligatable nick during lagging-strand DNA replication
    • Garg P, Stith CM, Sabouri N, Johansson E, Burgers PM. 2004. Idling by DNA polymerase δ maintains a ligatable nick during lagging-strand DNA replication. Genes Dev 18: 2764-2773.
    • (2004) Genes Dev , vol.18 , pp. 2764-2773
    • Garg, P.1    Stith, C.M.2    Sabouri, N.3    Johansson, E.4    Burgers, P.M.5
  • 8
    • 84910679960 scopus 로고    scopus 로고
    • A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions
    • Gilbert TM, McDaniel SL, Byrum SD, Cades JA, Dancy BC, Wade H, Tackett AJ, Strahl BD, Taverna SD. 2014. A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions. Mol Cell Proteomics 13: 2883-2895.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 2883-2895
    • Gilbert, T.M.1    McDaniel, S.L.2    Byrum, S.D.3    Cades, J.A.4    Dancy, B.C.5    Wade, H.6    Tackett, A.J.7    Strahl, B.D.8    Taverna, S.D.9
  • 9
    • 84898887583 scopus 로고    scopus 로고
    • A genetic screen based on in vivo RNA imaging reveals centrosome-independent mechanisms for localizing gurken transcripts in Drosophila
    • Hayashi R, Wainwright SM, Liddell SJ, Pinchin SM, Horswell S, Ish-Horowicz D. 2014. A genetic screen based on in vivo RNA imaging reveals centrosome-independent mechanisms for localizing gurken transcripts in Drosophila. G3 (Bethesda) 4: 749-760.
    • (2014) G3 (Bethesda) , vol.4 , pp. 749-760
    • Hayashi, R.1    Wainwright, S.M.2    Liddell, S.J.3    Pinchin, S.M.4    Horswell, S.5    Ish-Horowicz, D.6
  • 10
    • 34247198831 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor Dacapo promotes replication licensing during Drosophila endocycles
    • Hong A, Narbonne-Reveau K, Riesgo-Escovar J, Fu H, Aladjem MI, Lilly MA. 2007. The cyclin-dependent kinase inhibitor Dacapo promotes replication licensing during Drosophila endocycles. EMBO J 26: 2071-2082.
    • (2007) EMBO J , vol.26 , pp. 2071-2082
    • Hong, A.1    Narbonne-Reveau, K.2    Riesgo-Escovar, J.3    Fu, H.4    Aladjem, M.I.5    Lilly, M.A.6
  • 11
    • 0035577668 scopus 로고    scopus 로고
    • Histone H3 specific acetyltransferases are essential for cell cycle progression
    • Howe L, Auston D, Grant P, John S, Cook RG, Workman JL, Pillus L. 2001. Histone H3 specific acetyltransferases are essential for cell cycle progression. Genes Dev 15: 3144-3154.
    • (2001) Genes Dev , vol.15 , pp. 3144-3154
    • Howe, L.1    Auston, D.2    Grant, P.3    John, S.4    Cook, R.G.5    Workman, J.L.6    Pillus, L.7
  • 12
    • 84918546515 scopus 로고    scopus 로고
    • Histone acetyltransferase Enok regulates oocyte polarization by promoting expression of the actin nucleation factor spire
    • Huang F, Paulson A, Dutta A, Venkatesh S, Smolle M, Abmayr SM, Workman JL. 2014. Histone acetyltransferase Enok regulates oocyte polarization by promoting expression of the actin nucleation factor spire. Genes Dev 28: 2750-2763.
    • (2014) Genes Dev , vol.28 , pp. 2750-2763
    • Huang, F.1    Paulson, A.2    Dutta, A.3    Venkatesh, S.4    Smolle, M.5    Abmayr, S.M.6    Workman, J.L.7
  • 13
    • 0034657420 scopus 로고    scopus 로고
    • The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAFII30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex
    • John S, Howe L, Tafrov ST, Grant PA, Sternglanz R, Workman JL. 2000. The something about silencing protein, Sas3, is the catalytic subunit of NuA3, a yTAFII30-containing HAT complex that interacts with the Spt16 subunit of the yeast CP (Cdc68/Pob3)-FACT complex. Genes Dev 14: 1196-1208.
    • (2000) Genes Dev , vol.14 , pp. 1196-1208
    • John, S.1    Howe, L.2    Tafrov, S.T.3    Grant, P.A.4    Sternglanz, R.5    Workman, J.L.6
  • 14
    • 0141504148 scopus 로고    scopus 로고
    • Elg1 forms an alternative PCNA-interacting RFC complex required to maintain genome stability
    • Kanellis P, Agyei R, Durocher D. 2003. Elg1 forms an alternative PCNA-interacting RFC complex required to maintain genome stability. Curr Biol 13: 1583-1595.
    • (2003) Curr Biol , vol.13 , pp. 1583-1595
    • Kanellis, P.1    Agyei, R.2    Durocher, D.3
  • 15
    • 0242709317 scopus 로고    scopus 로고
    • Genome stability: A new member of the RFC family
    • Kim J, MacNeill SA. 2003. Genome stability: a new member of the RFC family. Curr Biol 13: R873-875.
    • (2003) Curr Biol , vol.13 , pp. R873-R875
    • Kim, J.1    Macneill, S.A.2
  • 16
    • 84876837172 scopus 로고    scopus 로고
    • The Elg1 replication factor C-like complex functions in PCNA unloading during DNA replication
    • Kubota T, Nishimura K, Kanemaki MT, Donaldson AD. 2013. The Elg1 replication factor C-like complex functions in PCNA unloading during DNA replication. Mol Cell 50: 273-280.
    • (2013) Mol Cell , vol.50 , pp. 273-280
    • Kubota, T.1    Nishimura, K.2    Kanemaki, M.T.3    Donaldson, A.D.4
  • 17
    • 84938554960 scopus 로고    scopus 로고
    • Replication-coupled PCNA unloading by the Elg1 complex occurs genome-wide and requires Okazaki fragment ligation
    • Kubota T, Katou Y, Nakato R, Shirahige K, Donaldson AD. 2015. Replication-coupled PCNA unloading by the Elg1 complex occurs genome-wide and requires Okazaki fragment ligation. Cell Rep 12: 774-787.
    • (2015) Cell Rep , vol.12 , pp. 774-787
    • Kubota, T.1    Katou, Y.2    Nakato, R.3    Shirahige, K.4    Donaldson, A.D.5
  • 19
    • 77951210668 scopus 로고    scopus 로고
    • Human ELG1 regulates the level of ubiquitinated proliferating cell nuclear antigen (PCNA) through Its interactions with PCNA and USP1
    • Lee KY, Yang K, Cohn MA, Sikdar N, D’Andrea AD, Myung K. 2010. Human ELG1 regulates the level of ubiquitinated proliferating cell nuclear antigen (PCNA) through Its interactions with PCNA and USP1. J Biol Chem 285: 10362-10369.
    • (2010) J Biol Chem , vol.285 , pp. 10362-10369
    • Lee, K.Y.1    Yang, K.2    Cohn, M.A.3    Sikdar, N.4    D’Andrea, A.D.5    Myung, K.6
  • 20
    • 84872087979 scopus 로고    scopus 로고
    • ATAD5 regulates the lifespan of DNA replication factories by modulating PCNA level on the chromatin
    • Lee KY, Fu H, Aladjem MI, Myung K. 2013. ATAD5 regulates the lifespan of DNA replication factories by modulating PCNA level on the chromatin. J Cell Biol 200: 31-44.
    • (2013) J Cell Biol , vol.200 , pp. 31-44
    • Lee, K.Y.1    Fu, H.2    Aladjem, M.I.3    Myung, K.4
  • 21
    • 0029802648 scopus 로고    scopus 로고
    • The Drosophila endocycle is controlled by Cyclin E and lacks a checkpoint ensuring S-phase completion
    • Lilly MA, Spradling AC. 1996. The Drosophila endocycle is controlled by Cyclin E and lacks a checkpoint ensuring S-phase completion. Genes Dev 10: 2514-2526.
    • (1996) Genes Dev , vol.10 , pp. 2514-2526
    • Lilly, M.A.1    Spradling, A.C.2
  • 22
    • 10644297436 scopus 로고    scopus 로고
    • Coordination of replication and transcription along a Drosophila chromosome
    • MacAlpine DM, Rodriguez HK, Bell SP. 2004. Coordination of replication and transcription along a Drosophila chromosome. Genes Dev 18: 3094-3105.
    • (2004) Genes Dev , vol.18 , pp. 3094-3105
    • Macalpine, D.M.1    Rodriguez, H.K.2    Bell, S.P.3
  • 23
    • 11144266855 scopus 로고    scopus 로고
    • The PCNA-RFC families of DNA clamps and clamp loaders
    • Majka J, Burgers PM. 2004. The PCNA-RFC families of DNA clamps and clamp loaders. Prog Nucleic Acid Res Mol Biol 78: 227-260.
    • (2004) Prog Nucleic Acid Res Mol Biol , vol.78 , pp. 227-260
    • Majka, J.1    Burgers, P.M.2
  • 24
    • 0036684101 scopus 로고    scopus 로고
    • Comparison of three directly coupled HPLC MS/MS strategies for identification of proteins from complex mixtures: Single-dimension LC-MS/MS, 2-phase MudPIT, and 3- phase MudPIT
    • McDonalda WH, Ohib R, Miyamotob DT, Mitchison TJ, Yates JR. 2002. Comparison of three directly coupled HPLC MS/MS strategies for identification of proteins from complex mixtures: single-dimension LC-MS/MS, 2-phase MudPIT, and 3- phase MudPIT. Int J Mass Spectrom 219: 245-251.
    • (2002) Int J Mass Spectrom , vol.219 , pp. 245-251
    • McDonalda, W.H.1    Ohib, R.2    Miyamotob, D.T.3    Mitchison, T.J.4    Yates, J.R.5
  • 25
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the maestro of the replication fork
    • Moldovan GL, Pfander B, Jentsch S. 2007. PCNA, the maestro of the replication fork. Cell 129: 665-679.
    • (2007) Cell , vol.129 , pp. 665-679
    • Moldovan, G.L.1    Pfander, B.2    Jentsch, S.3
  • 28
    • 66549126667 scopus 로고    scopus 로고
    • The histone acetyl transferase activity of monocytic leukemia zinc finger is critical for the proliferation of hematopoietic precursors
    • Perez-Campo FM, Borrow J, Kouskoff V, Lacaud G. 2009. The histone acetyl transferase activity of monocytic leukemia zinc finger is critical for the proliferation of hematopoietic precursors. Blood 113: 4866-4874.
    • (2009) Blood , vol.113 , pp. 4866-4874
    • Perez-Campo, F.M.1    Borrow, J.2    Kouskoff, V.3    Lacaud, G.4
  • 30
    • 58649114520 scopus 로고    scopus 로고
    • Monocytic leukemia zinc finger (MOZ) interacts with p53 to induce p21 expression and cell-cycle arrest
    • Rokudai S, Aikawa Y, Tagata Y, Tsuchida N, Taya Y, Kitabayashi I. 2009. Monocytic leukemia zinc finger (MOZ) interacts with p53 to induce p21 expression and cell-cycle arrest. J Biol Chem 284: 237-244.
    • (2009) J Biol Chem , vol.284 , pp. 237-244
    • Rokudai, S.1    Aikawa, Y.2    Tagata, Y.3    Tsuchida, N.4    Taya, Y.5    Kitabayashi, I.6
  • 31
    • 84874594177 scopus 로고    scopus 로고
    • MOZincreases p53 acetylation and premature senescence through its complex formation with PML
    • Rokudai S, Laptenko O, Arnal SM, Taya Y, Kitabayashi I, Prives C. 2013.MOZincreases p53 acetylation and premature senescence through its complex formation with PML. Proc Natl Acad Sci 110: 3895-3900.
    • (2013) Proc Natl Acad Sci , vol.110 , pp. 3895-3900
    • Rokudai, S.1    Laptenko, O.2    Arnal, S.M.3    Taya, Y.4    Kitabayashi, I.5    Prives, C.6
  • 32
    • 0036894133 scopus 로고    scopus 로고
    • The E2F cell cycle regulator is required for Drosophila nurse cell DNA replication and apoptosis
    • Royzman I, Hayashi-Hagihara A, Dej KJ, Bosco G, Lee JY, Orr-Weaver TL. 2002. The E2F cell cycle regulator is required for Drosophila nurse cell DNA replication and apoptosis. Mech Dev 119: 225-237.
    • (2002) Mech Dev , vol.119 , pp. 225-237
    • Royzman, I.1    Hayashi-Hagihara, A.2    Dej, K.J.3    Bosco, G.4    Lee, J.Y.5    Orr-Weaver, T.L.6
  • 33
    • 0035936579 scopus 로고    scopus 로고
    • Enok encodes a Drosophila putative histone acetyltransferase required for mushroom body neuroblast proliferation
    • Scott EK, Lee T, Luo L. 2001. Enok encodes a Drosophila putative histone acetyltransferase required for mushroom body neuroblast proliferation. Curr Biol 11: 99-104.
    • (2001) Curr Biol , vol.11 , pp. 99-104
    • Scott, E.K.1    Lee, T.2    Luo, L.3
  • 34
    • 3042847983 scopus 로고    scopus 로고
    • The mitotic-to-endocycle switch in Drosophila follicle cells is executed by Notch-dependent regulation of G1/S, G2/M and M/G1 cell-cycle transitions
    • Shcherbata HR, Althauser C, Findley SD, Ruohola-Baker H. 2004. The mitotic-to-endocycle switch in Drosophila follicle cells is executed by Notch-dependent regulation of G1/S, G2/M and M/G1 cell-cycle transitions. Development 131: 3169-3181.
    • (2004) Development , vol.131 , pp. 3169-3181
    • Shcherbata, H.R.1    Althauser, C.2    Findley, S.D.3    Ruohola-Baker, H.4
  • 36
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb DL, McDonald WH, Yates JR III. 2002. DTASelect and Contrast: tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res 1: 21-26.
    • (2002) J Proteome Res , vol.1 , pp. 21-26
    • Tabb, D.L.1    McDonald, W.H.2    Yates, J.3
  • 37
    • 33751527233 scopus 로고    scopus 로고
    • Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3HATactivity at K14 of H3 and transcription at a subset of targeted ORFs
    • Taverna SD, Ilin S, Rogers RS, Tanny JC, Lavender H, Li H, Baker L, Boyle J, Blair LP, Chait BT, et al. 2006. Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3HATactivity at K14 of H3 and transcription at a subset of targeted ORFs. Mol Cell 24: 785-796.
    • (2006) Mol Cell , vol.24 , pp. 785-796
    • Taverna, S.D.1    Ilin, S.2    Rogers, R.S.3    Tanny, J.C.4    Lavender, H.5    Li, H.6    Baker, L.7    Boyle, J.8    Blair, L.P.9    Chait, B.T.10
  • 39
    • 1842375739 scopus 로고    scopus 로고
    • SWI/SNF stimulates the formation of disparate activator-nucleosome complexes but is partially redundant with cooperative binding
    • Utley RT, Cote J, Owen-Hughes T, Workman JL. 1997. SWI/SNF stimulates the formation of disparate activator-nucleosome complexes but is partially redundant with cooperative binding. J Biol Chem 272: 12642-12649.
    • (1997) J Biol Chem , vol.272 , pp. 12642-12649
    • Utley, R.T.1    Cote, J.2    Owen-Hughes, T.3    Workman, J.L.4
  • 41
    • 84912049472 scopus 로고    scopus 로고
    • Comprehensive analysis of interacting proteins and genome-wide location studies of the Sas3-dependent NuA3 histone acetyltransferase complex
    • Vicente-Munoz S, Romero P, Magraner-Pardo L, Martinez-Jimenez CP, Tordera V, Pamblanco M. 2014. Comprehensive analysis of interacting proteins and genome-wide location studies of the Sas3-dependent NuA3 histone acetyltransferase complex. FEBS Open Bio 4: 996-1006.
    • (2014) FEBS Open Bio , vol.4 , pp. 996-1006
    • Vicente-Munoz, S.1    Romero, P.2    Magraner-Pardo, L.3    Martinez-Jimenez, C.P.4    Tordera, V.5    Pamblanco, M.6
  • 42
    • 34547895492 scopus 로고    scopus 로고
    • MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells
    • Yang XJ, Ullah M. 2007. MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells. Oncogene 26: 5408-5419.
    • (2007) Oncogene , vol.26 , pp. 5408-5419
    • Yang, X.J.1    Ullah, M.2
  • 43
    • 77949795829 scopus 로고    scopus 로고
    • Refinements to label free proteome quantitation: How to deal with peptides shared by multiple proteins
    • Zhang Y, Wen Z, Washburn MP, Florens L. 2010. Refinements to label free proteome quantitation: how to deal with peptides shared by multiple proteins. Anal Chem 82: 2272-2281.
    • (2010) Anal Chem , vol.82 , pp. 2272-2281
    • Zhang, Y.1    Wen, Z.2    Washburn, M.P.3    Florens, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.