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Volumn 48, Issue 3, 2012, Pages 459-470

The p23 Molecular Chaperone and GCN5 Acetylase Jointly Modulate Protein-DNA Dynamics and Open Chromatin Status

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE ACETYLTRANSFERASE GCN5; LYSINE; PROTEIN P23; TRANSCRIPTION FACTOR;

EID: 84869086668     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2012.08.026     Document Type: Article
Times cited : (35)

References (48)
  • 1
    • 0035997368 scopus 로고    scopus 로고
    • DNA replication in eukaryotic cells
    • Bell S.P., Dutta A. DNA replication in eukaryotic cells. Annu. Rev. Biochem. 2002, 71:333-374.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 333-374
    • Bell, S.P.1    Dutta, A.2
  • 3
    • 34247646897 scopus 로고    scopus 로고
    • Loss of Gcn5 acetyltransferase activity leads to neural tube closure defects and exencephaly in mouse embryos
    • Bu P., Evrard Y.A., Lozano G., Dent S.Y. Loss of Gcn5 acetyltransferase activity leads to neural tube closure defects and exencephaly in mouse embryos. Mol. Cell. Biol. 2007, 27:3405-3416.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3405-3416
    • Bu, P.1    Evrard, Y.A.2    Lozano, G.3    Dent, S.Y.4
  • 4
    • 43549102208 scopus 로고    scopus 로고
    • HSP90: the Rosetta stone for cellular protein dynamics?
    • DeZwaan D.C., Freeman B.C. HSP90: the Rosetta stone for cellular protein dynamics?. Cell Cycle 2008, 7:1006-1012.
    • (2008) Cell Cycle , vol.7 , pp. 1006-1012
    • DeZwaan, D.C.1    Freeman, B.C.2
  • 6
    • 67650337568 scopus 로고    scopus 로고
    • The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states
    • DeZwaan D.C., Toogun O.A., Echtenkamp F.J., Freeman B.C. The Hsp82 molecular chaperone promotes a switch between unextendable and extendable telomere states. Nat. Struct. Mol. Biol. 2009, 16:711-716.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 711-716
    • DeZwaan, D.C.1    Toogun, O.A.2    Echtenkamp, F.J.3    Freeman, B.C.4
  • 7
    • 84857058279 scopus 로고    scopus 로고
    • Expanding the cellular molecular chaperone network through the ubiquitous cochaperones
    • Echtenkamp F.J., Freeman B.C. Expanding the cellular molecular chaperone network through the ubiquitous cochaperones. Biochim. Biophys. Acta 2012, 1823:668-673.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 668-673
    • Echtenkamp, F.J.1    Freeman, B.C.2
  • 9
  • 10
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis J. Proteins as molecular chaperones. Nature 1987, 328:378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 11
    • 77952520644 scopus 로고    scopus 로고
    • GCN5 is a positive regulator of origins of DNA replication in Saccharomyces cerevisiae
    • Espinosa M.C., Rehman M.A., Chisamore-Robert P., Jeffery D., Yankulov K. GCN5 is a positive regulator of origins of DNA replication in Saccharomyces cerevisiae. PLoS ONE 2010, 5:e8964. 10.1371/journal.pone.0008964.
    • (2010) PLoS ONE , vol.5
    • Espinosa, M.C.1    Rehman, M.A.2    Chisamore-Robert, P.3    Jeffery, D.4    Yankulov, K.5
  • 12
    • 0035338418 scopus 로고    scopus 로고
    • Continuous recycling: a mechanism for modulatory signal transduction
    • Freeman B.C., Yamamoto K.R. Continuous recycling: a mechanism for modulatory signal transduction. Trends Biochem. Sci. 2001, 26:285-290.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 285-290
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 13
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman B.C., Yamamoto K.R. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 2002, 296:2232-2235.
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 14
    • 0034102339 scopus 로고    scopus 로고
    • The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
    • Freeman B.C., Felts S.J., Toft D.O., Yamamoto K.R. The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. Genes Dev. 2000, 14:422-434.
    • (2000) Genes Dev. , vol.14 , pp. 422-434
    • Freeman, B.C.1    Felts, S.J.2    Toft, D.O.3    Yamamoto, K.R.4
  • 17
    • 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., Duggan L., Côté J., Roberts S.M., Brownell J.E., Candau R., Ohba R., Owen-Hughes T., Allis C.D., Winston F., 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. 1997, 11:1640-1650.
    • (1997) Genes Dev. , vol.11 , pp. 1640-1650
    • Grant, P.A.1    Duggan, L.2    Côté, J.3    Roberts, S.M.4    Brownell, J.E.5    Candau, R.6    Ohba, R.7    Owen-Hughes, T.8    Allis, C.D.9    Winston, F.10
  • 20
    • 0029835806 scopus 로고    scopus 로고
    • GCN5p, a yeast nuclear histone acetyltransferase, acetylates specific lysines in histone H3 and H4 that differ from deposition-related acetylation sites
    • Kuo M.H., Brownell J.E., Sobel R.E., Ranalli T.A., Cook R.G., Edmonson D.G., Roth S.Y., Allis C.D. GCN5p, a yeast nuclear histone acetyltransferase, acetylates specific lysines in histone H3 and H4 that differ from deposition-related acetylation sites. Nature 1996, 383:269-272.
    • (1996) Nature , vol.383 , pp. 269-272
    • Kuo, M.H.1    Brownell, J.E.2    Sobel, R.E.3    Ranalli, T.A.4    Cook, R.G.5    Edmonson, D.G.6    Roth, S.Y.7    Allis, C.D.8
  • 21
    • 0034667792 scopus 로고    scopus 로고
    • Orchestrated response: a symphony of transcription factors for gene control
    • Lemon B., Tjian R. Orchestrated response: a symphony of transcription factors for gene control. Genes Dev. 2000, 14:2551-2569.
    • (2000) Genes Dev. , vol.14 , pp. 2551-2569
    • Lemon, B.1    Tjian, R.2
  • 22
    • 0036136341 scopus 로고    scopus 로고
    • Characterization of the ECB binding complex responsible for the M/G(1)-specific transcription of CLN3 and SWI4
    • Mai B., Miles S., Breeden L.L. Characterization of the ECB binding complex responsible for the M/G(1)-specific transcription of CLN3 and SWI4. Mol. Cell. Biol. 2002, 22:430-441.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 430-441
    • Mai, B.1    Miles, S.2    Breeden, L.L.3
  • 23
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: rapid exchange with regulatory sites in living cells
    • McNally J.G., Müller W.G., Walker D., Wolford R., Hager G.L. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science 2000, 287:1262-1265.
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Müller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5
  • 24
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Métivier R., Penot G., Hübner M.R., Reid G., Brand H., Kos M., Gannon F. Estrogen receptor-α directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 2003, 115:751-763.
    • (2003) Cell , vol.115 , pp. 751-763
    • Métivier, R.1    Penot, G.2    Hübner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 25
    • 0035889085 scopus 로고    scopus 로고
    • The concept of self-organization in cellular architecture
    • Misteli T. The concept of self-organization in cellular architecture. J. Cell Biol. 2001, 155:181-185.
    • (2001) J. Cell Biol. , vol.155 , pp. 181-185
    • Misteli, T.1
  • 26
    • 0023815651 scopus 로고
    • Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells
    • Mosser D.D., Theodorakis N.G., Morimoto R.I. Coordinate changes in heat shock element-binding activity and HSP70 gene transcription rates in human cells. Mol. Cell. Biol. 1988, 8:4736-4744.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4736-4744
    • Mosser, D.D.1    Theodorakis, N.G.2    Morimoto, R.I.3
  • 27
    • 0042567276 scopus 로고    scopus 로고
    • Inhibition of MMTV transcription by HDAC inhibitors occurs independent of changes in chromatin remodeling and increased histone acetylation
    • Mulholland N.M., Soeth E., Smith C.L. Inhibition of MMTV transcription by HDAC inhibitors occurs independent of changes in chromatin remodeling and increased histone acetylation. Oncogene 2003, 22:4807-4818.
    • (2003) Oncogene , vol.22 , pp. 4807-4818
    • Mulholland, N.M.1    Soeth, E.2    Smith, C.L.3
  • 28
    • 34547864553 scopus 로고    scopus 로고
    • Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation
    • Nagy Z., Tora L. Distinct GCN5/PCAF-containing complexes function as co-activators and are involved in transcription factor and global histone acetylation. Oncogene 2007, 26:5341-5357.
    • (2007) Oncogene , vol.26 , pp. 5341-5357
    • Nagy, Z.1    Tora, L.2
  • 29
    • 0033178880 scopus 로고    scopus 로고
    • New yeast genes important for chromosome integrity and segregation identified by dosage effects on genome stability
    • Ouspenski I.I., Elledge S.J., Brinkley B.R. New yeast genes important for chromosome integrity and segregation identified by dosage effects on genome stability. Nucleic Acids Res. 1999, 27:3001-3008.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3001-3008
    • Ouspenski, I.I.1    Elledge, S.J.2    Brinkley, B.R.3
  • 31
    • 0025007114 scopus 로고
    • Quantitative analysis of the glucocorticoid receptor-DNA interaction at the mouse mammary tumor virus glucocorticoid response element
    • Perlmann T., Eriksson P., Wrange O. Quantitative analysis of the glucocorticoid receptor-DNA interaction at the mouse mammary tumor virus glucocorticoid response element. J. Biol. Chem. 1990, 265:17222-17229.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17222-17229
    • Perlmann, T.1    Eriksson, P.2    Wrange, O.3
  • 32
    • 3042760021 scopus 로고    scopus 로고
    • Global nature of dynamic protein-chromatin interactions in vivo: three-dimensional genome scanning and dynamic interaction networks of chromatin proteins
    • Phair R.D., Scaffidi P., Elbi C., Vecerová J., Dey A., Ozato K., Brown D.T., Hager G., Bustin M., Misteli T. Global nature of dynamic protein-chromatin interactions in vivo: three-dimensional genome scanning and dynamic interaction networks of chromatin proteins. Mol. Cell. Biol. 2004, 24:6393-6402.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6393-6402
    • Phair, R.D.1    Scaffidi, P.2    Elbi, C.3    Vecerová, J.4    Dey, A.5    Ozato, K.6    Brown, D.T.7    Hager, G.8    Bustin, M.9    Misteli, T.10
  • 36
    • 0025989349 scopus 로고
    • Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability
    • Sarge K.D., Zimarino V., Holm K., Wu C., Morimoto R.I. Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNA-binding ability. Genes Dev. 1991, 5:1902-1911.
    • (1991) Genes Dev. , vol.5 , pp. 1902-1911
    • Sarge, K.D.1    Zimarino, V.2    Holm, K.3    Wu, C.4    Morimoto, R.I.5
  • 37
    • 0029025078 scopus 로고
    • The carboxyl-terminal transactivation domain of heat shock factor 1 is negatively regulated and stress responsive
    • Shi Y., Kroeger P.E., Morimoto R.I. The carboxyl-terminal transactivation domain of heat shock factor 1 is negatively regulated and stress responsive. Mol. Cell. Biol. 1995, 15:4309-4318.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4309-4318
    • Shi, Y.1    Kroeger, P.E.2    Morimoto, R.I.3
  • 38
    • 52449132322 scopus 로고    scopus 로고
    • Is there a code embedded in proteins that is based on post-translational modifications?
    • Sims R.J., Reinberg D. Is there a code embedded in proteins that is based on post-translational modifications?. Nat. Rev. Mol. Cell Biol. 2008, 9:815-820.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 815-820
    • Sims, R.J.1    Reinberg, D.2
  • 39
    • 34347249238 scopus 로고    scopus 로고
    • The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation
    • Toogun O.A., Zeiger W., Freeman B.C. The p23 molecular chaperone promotes functional telomerase complexes through DNA dissociation. Proc. Nat.l Acad. Sci. USA 2007, 104:5765-5770.
    • (2007) Proc. Nat.l Acad. Sci. USA , vol.104 , pp. 5765-5770
    • Toogun, O.A.1    Zeiger, W.2    Freeman, B.C.3
  • 40
    • 37549046440 scopus 로고    scopus 로고
    • The Hsp90 molecular chaperone modulates multiple telomerase activities
    • Toogun O.A., DeZwaan D.C., Freeman B.C. The Hsp90 molecular chaperone modulates multiple telomerase activities. Mol. Cell. Biol. 2008, 28:457-467.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 457-467
    • Toogun, O.A.1    DeZwaan, D.C.2    Freeman, B.C.3
  • 41
    • 0021268344 scopus 로고
    • Early events in the stimulation of mammary tumor virus RNA synthesis by glucocorticoids. Novel assays of transcription rates
    • Ucker D.S., Yamamoto K.R. Early events in the stimulation of mammary tumor virus RNA synthesis by glucocorticoids. Novel assays of transcription rates. J. Biol. Chem. 1984, 259:7416-7420.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7416-7420
    • Ucker, D.S.1    Yamamoto, K.R.2
  • 42
    • 0034725641 scopus 로고    scopus 로고
    • Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone
    • Weaver A.J., Sullivan W.P., Felts S.J., Owen B.A., Toft D.O. Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J. Biol. Chem. 2000, 275:23045-23052.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23045-23052
    • Weaver, A.J.1    Sullivan, W.P.2    Felts, S.J.3    Owen, B.A.4    Toft, D.O.5
  • 43
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • Westerheide S.D., Anckar J., Stevens S.M., Sistonen L., Morimoto R.I. Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 2009, 323:1063-1066.
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens, S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 44
    • 0022327612 scopus 로고
    • Steroid receptor regulated transcription of specific genes and gene networks
    • Yamamoto K.R. Steroid receptor regulated transcription of specific genes and gene networks. Annu. Rev. Genet. 1985, 19:209-252.
    • (1985) Annu. Rev. Genet. , vol.19 , pp. 209-252
    • Yamamoto, K.R.1
  • 46
    • 49349107518 scopus 로고    scopus 로고
    • Lysine acetylation: codified crosstalk with other posttranslational modifications
    • Yang X.J., Seto E. Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol. Cell 2008, 31:449-461.
    • (2008) Mol. Cell , vol.31 , pp. 449-461
    • Yang, X.J.1    Seto, E.2
  • 47
    • 0021745342 scopus 로고
    • Reversible and persistent changes in chromatin structure accompany activation of a glucocorticoid-dependent enhancer element
    • Zaret K.S., Yamamoto K.R. Reversible and persistent changes in chromatin structure accompany activation of a glucocorticoid-dependent enhancer element. Cell 1984, 38:29-38.
    • (1984) Cell , vol.38 , pp. 29-38
    • Zaret, K.S.1    Yamamoto, K.R.2
  • 48
    • 0032723678 scopus 로고    scopus 로고
    • Identification of target sites of the alpha2-Mcm1 repressor complex in the yeast genome
    • Zhong H., McCord R., Vershon A.K. Identification of target sites of the alpha2-Mcm1 repressor complex in the yeast genome. Genome Res. 1999, 9:1040-1047.
    • (1999) Genome Res. , vol.9 , pp. 1040-1047
    • Zhong, H.1    McCord, R.2    Vershon, A.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.