메뉴 건너뛰기




Volumn 289, Issue 44, 2014, Pages 30459-30469

Genomic heat shock element sequences drive cooperative human heat shock factor 1 DNA binding and selectivity

Author keywords

[No Author keywords available]

Indexed keywords

DNA; DNA BINDING PROTEIN; HEAT SHOCK TRANSCRIPTION FACTOR; PROTEIN BINDING; TRANSCRIPTION FACTOR;

EID: 84908689538     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.591578     Document Type: Article
Times cited : (53)

References (34)
  • 1
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B., Weissman, J., and Horwich, A. (2006) Molecular chaperones and protein quality control. Cell 125, 443-451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 2
    • 82455210670 scopus 로고    scopus 로고
    • Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases
    • Neef, D. W., Jaeger, A. M., and Thiele, D. J. (2011) Heat shock transcription factor 1 as a therapeutic target in neurodegenerative diseases. Nat. Rev. Drug Discov. 10, 930-944
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 930-944
    • Neef, D.W.1    Jaeger, A.M.2    Thiele, D.J.3
  • 3
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: Integrators of cell stress, development, and lifespan
    • Akerfelt, M., Morimoto, R. I., and Sistonen, L. (2010) Heat shock factors: integrators of cell stress, development, and lifespan. Nat. Rev. Mol. Cell Biol. 11, 545-555
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 4
    • 84884695800 scopus 로고    scopus 로고
    • Integration of the unfolded protein and oxidative stress responses through SKN-1/Nrf
    • Glover-Cutter, K. M., Lin, S., and Blackwell, T. K. (2013) Integration of the unfolded protein and oxidative stress responses through SKN-1/Nrf. PLoS Genet. 9, e1003701
    • (2013) PLoS Genet. , vol.9 , pp. e1003701
    • Glover-Cutter, K.M.1    Lin, S.2    Blackwell, T.K.3
  • 5
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto, R. I. (2008) Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 22, 1427-1438
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 6
    • 0031297298 scopus 로고    scopus 로고
    • The heat-shock response: Regulation and function of heat-shock proteins and molecular chaperones
    • Morimoto, R. I., Kline, M. P., Bimston, D. N., and Cotto, J. J. (1997) The heat-shock response: regulation and function of heat-shock proteins and molecular chaperones. Essays Biochem. 32, 17-29
    • (1997) Essays Biochem. , vol.32 , pp. 17-29
    • Morimoto, R.I.1    Kline, M.P.2    Bimston, D.N.3    Cotto, J.J.4
  • 7
    • 68649113747 scopus 로고    scopus 로고
    • The role of molecular chaperones in human misfolding diseases
    • Broadley, S. A., and Hartl, F. U. (2009) The role of molecular chaperones in human misfolding diseases. FEBS Lett. 583, 2647-2653
    • (2009) FEBS Lett. , vol.583 , pp. 2647-2653
    • Broadley, S.A.1    Hartl, F.U.2
  • 8
    • 0036501074 scopus 로고    scopus 로고
    • Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy
    • Bailey, C. K., Andriola, I. F., Kampinga, H. H., and Merry, D. E. (2002) Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophy. Hum. Mol. Genet. 11, 515-523
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 515-523
    • Bailey, C.K.1    Andriola, I.F.2    Kampinga, H.H.3    Merry, D.E.4
  • 10
    • 2942598422 scopus 로고    scopus 로고
    • Genome-wide analysis of the biology of stress responses through heat shock transcription factor
    • Hahn, J. S., Hu, Z., Thiele, D. J., and Iyer, V. R. (2004) Genome-wide analysis of the biology of stress responses through heat shock transcription factor. Mol. Cell. Biol. 24, 5249-5256
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 5249-5256
    • Hahn, J.S.1    Hu, Z.2    Thiele, D.J.3    Iyer, V.R.4
  • 11
    • 0035824621 scopus 로고    scopus 로고
    • Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex
    • Guo, Y., Guettouche, T., Fenna, M., Boellmann, F., Pratt, W. B., Toft, D. O., Smith, D. F., and Voellmy, R. (2001) Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. J. Biol. Chem. 276, 45791-45799
    • (2001) J. Biol. Chem. , vol.276 , pp. 45791-45799
    • Guo, Y.1    Guettouche, T.2    Fenna, M.3    Boellmann, F.4    Pratt, W.B.5    Toft, D.O.6    Smith, D.F.7    Voellmy, R.8
  • 12
    • 0031931412 scopus 로고    scopus 로고
    • Intramolecular repression of mouse heat shock factor 1
    • Farkas, T., Kutskova, Y. A., and Zimarino, V. (1998) Intramolecular repression of mouse heat shock factor 1. Mol. Cell. Biol. 18, 906-918
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 906-918
    • Farkas, T.1    Kutskova, Y.A.2    Zimarino, V.3
  • 13
    • 0027452754 scopus 로고
    • Regulation of heat shock factor trimer formation: Role of a conserved leucine zipper
    • Rabindran, S. K., Haroun, R. I., Clos, J., Wisniewski, J., and Wu, C. (1993) Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science 259, 230-234
    • (1993) Science , vol.259 , pp. 230-234
    • Rabindran, S.K.1    Haroun, R.I.2    Clos, J.3    Wisniewski, J.4    Wu, C.5
  • 14
    • 0020184673 scopus 로고
    • A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene
    • Pelham, H. R. (1982) A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene. Cell 30, 517-528
    • (1982) Cell , vol.30 , pp. 517-528
    • Pelham, H.R.1
  • 16
    • 84859230739 scopus 로고    scopus 로고
    • Accurate prediction of inducible transcription factor binding intensities in vivo
    • Guertin, M. J., Martins, A. L., Siepel, A., and Lis, J. T. (2012) Accurate prediction of inducible transcription factor binding intensities in vivo. PLoS Genet. 8, e1002610
    • (2012) PLoS Genet. , vol.8 , pp. e1002610
    • Guertin, M.J.1    Martins, A.L.2    Siepel, A.3    Lis, J.T.4
  • 17
    • 0037018158 scopus 로고    scopus 로고
    • In vivo binding of active heat shock transcription factor 1 to human chromosome 9 heterochromatin during stress
    • Jolly, C., Konecny, L., Grady, D. L., Kutskova, Y. A., Cotto, J. J., Morimoto, R. I., and Vourc'h, C. (2002) In vivo binding of active heat shock transcription factor 1 to human chromosome 9 heterochromatin during stress. J. Cell Biol. 156, 775-781
    • (2002) J. Cell Biol. , vol.156 , pp. 775-781
    • Jolly, C.1    Konecny, L.2    Grady, D.L.3    Kutskova, Y.A.4    Cotto, J.J.5    Morimoto, R.I.6    Vourc'h, C.7
  • 19
    • 36349036470 scopus 로고    scopus 로고
    • Heat shock transcription factor 1 opens chromatin structure of interleukin-6 promoter to facilitate binding of an activator or a repressor
    • Inouye, S., Fujimoto, M., Nakamura, T., Takaki, E., Hayashida, N., Hai, T., and Nakai, A. (2007) Heat shock transcription factor 1 opens chromatin structure of interleukin-6 promoter to facilitate binding of an activator or a repressor. J. Biol. Chem. 282, 33210-33217
    • (2007) J. Biol. Chem. , vol.282 , pp. 33210-33217
    • Inouye, S.1    Fujimoto, M.2    Nakamura, T.3    Takaki, E.4    Hayashida, N.5    Hai, T.6    Nakai, A.7
  • 20
    • 84876869300 scopus 로고    scopus 로고
    • Identification of a tissue-selective heat shock response regulatory network
    • Guisbert, E., Czyz, D. M., Richter, K., McMullen, P. D., and Morimoto, R. I. (2013) Identification of a tissue-selective heat shock response regulatory network. PLoS Genet. 9, e1003466
    • (2013) PLoS Genet. , vol.9 , pp. e1003466
    • Guisbert, E.1    Czyz, D.M.2    Richter, K.3    McMullen, P.D.4    Morimoto, R.I.5
  • 21
    • 0028586833 scopus 로고
    • Effects of neurohormonal stress and aging on the activation of mammalian heat shock factor 1
    • Fawcett, T. W., Sylvester, S. L., Sarge, K. D., Morimoto, R. I., and Holbrook, N. J. (1994) Effects of neurohormonal stress and aging on the activation of mammalian heat shock factor 1. J. Biol. Chem. 269, 32272-32278
    • (1994) J. Biol. Chem. , vol.269 , pp. 32272-32278
    • Fawcett, T.W.1    Sylvester, S.L.2    Sarge, K.D.3    Morimoto, R.I.4    Holbrook, N.J.5
  • 22
    • 0025300038 scopus 로고
    • In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation
    • Mosser, D. D., Kotzbauer, P. T., Sarge, K. D., and Morimoto, R. I. (1990) In vitro activation of heat shock transcription factor DNA-binding by calcium and biochemical conditions that affect protein conformation. Proc. Natl. Acad. Sci. U. S. A. 87, 3748-3752
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 3748-3752
    • Mosser, D.D.1    Kotzbauer, P.T.2    Sarge, K.D.3    Morimoto, R.I.4
  • 25
    • 0032936785 scopus 로고    scopus 로고
    • A new use for the 'wing' of the 'winged' helix-turn-helix motif in the HSF-DNA cocrystal
    • Littlefield, O., and Nelson, H. C. (1999) A new use for the 'wing' of the 'winged' helix-turn-helix motif in the HSF-DNA cocrystal. Nat. Struct. Biol. 6, 464-470
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 464-470
    • Littlefield, O.1    Nelson, H.C.2
  • 26
    • 0028150986 scopus 로고
    • Activation of the DNAbinding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure
    • Zuo, J., Baler, R., Dahl, G., and Voellmy, R. (1994) Activation of the DNAbinding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure. Mol. Cell. Biol. 14, 7557-7568
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7557-7568
    • Zuo, J.1    Baler, R.2    Dahl, G.3    Voellmy, R.4
  • 28
    • 43049095602 scopus 로고    scopus 로고
    • Methods for protein characterization by mass spectrometry, thermal shift (ThermoFluor) assay, and multiangle or static light scattering
    • Nettleship, J. E., Brown, J., Groves, M. R., and Geerlof, A. (2008) Methods for protein characterization by mass spectrometry, thermal shift (ThermoFluor) assay, and multiangle or static light scattering. Methods Mol. Biol. 426, 299-318
    • (2008) Methods Mol. Biol. , vol.426 , pp. 299-318
    • Nettleship, J.E.1    Brown, J.2    Groves, M.R.3    Geerlof, A.4
  • 29
    • 33749850046 scopus 로고    scopus 로고
    • Universal screening methods and applications of ThermoFluor
    • Cummings, M. D., Farnum, M. A., and Nelen, M. I. (2006) Universal screening methods and applications of ThermoFluor. J. Biomol. Screen. 11, 854-863
    • (2006) J. Biomol. Screen. , vol.11 , pp. 854-863
    • Cummings, M.D.1    Farnum, M.A.2    Nelen, M.I.3
  • 30
    • 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., Jr., Sistonen, L., and Morimoto, R. I. (2009) Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 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
  • 31
    • 0025965278 scopus 로고
    • Cooperative binding of Drosophila heat shock factor to arrays of a conserved 5 bp unit
    • Xiao, H., Perisic, O., and Lis, J. T. (1991) Cooperative binding of Drosophila heat shock factor to arrays of a conserved 5 bp unit. Cell 64, 585-593
    • (1991) Cell , vol.64 , pp. 585-593
    • Xiao, H.1    Perisic, O.2    Lis, J.T.3
  • 34
    • 0036901003 scopus 로고    scopus 로고
    • Multisite phosphorylation provides sophisticated regulation of transcription factors
    • Holmberg, C. I., Tran, S. E., Eriksson, J. E., and Sistonen, L. (2002) Multisite phosphorylation provides sophisticated regulation of transcription factors. Trends Biochem. Sci. 27, 619-627
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 619-627
    • Holmberg, C.I.1    Tran, S.E.2    Eriksson, J.E.3    Sistonen, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.