메뉴 건너뛰기




Volumn 287, Issue 32, 2012, Pages 26962-26970

Impact of protein/protein interactions on global intermolecular translocation rates of the transcription factors Sox2 and Oct1 between DNA cognate sites analyzed by z-exchange NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ADJACENT SITES; BINDING EVENTS; CONTACT SURFACE; DNA MOLECULES; FREE SOLUTIONS; HOMEODOMAIN; NO DISSOCIATION;

EID: 84864557450     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.382960     Document Type: Article
Times cited : (16)

References (37)
  • 1
    • 0033056554 scopus 로고    scopus 로고
    • Multiprotein·DNA complexes in transcriptional regulation
    • Wolberger, C. (1999) Multiprotein·DNA complexes in transcriptional regulation. Annu. Rev. Biophys. Biomol. Struct. 28, 29-56
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 29-56
    • Wolberger, C.1
  • 2
    • 0034175998 scopus 로고    scopus 로고
    • Pairing SOX off: With partners in the regulation of embryonic development
    • DOI 10.1016/S0168-9525(99)01955-1, PII S0168952599019551
    • Kamachi, Y., Uchikawa, M., and Kondoh, H. (2000) Pairing SOX off: with partners in the regulation of embryonic development. Trends Genet. 16, 182-187 (Pubitemid 30169154)
    • (2000) Trends in Genetics , vol.16 , Issue.4 , pp. 182-187
    • Kamachi, Y.1    Uchikawa, M.2    Kondoh, H.3
  • 3
    • 0035125506 scopus 로고    scopus 로고
    • Coevolution of HMG domains and homeodomains and the generation of transcriptional regulation by Sox/POU complexes
    • DOI 10.1002/1097-4652(2001)9999:9999<000::AID-JCP1046>3.0.CO;2-Y
    • Dailey, L., and Basilico, C. (2001) Coevolution of HMG domains and homeodomains and the generation of transcriptional regulation by Sox/POU complexes. J. Cell Physiol. 186, 315-328 (Pubitemid 32147715)
    • (2001) Journal of Cellular Physiology , vol.186 , Issue.3 , pp. 315-328
    • Dailey, L.1    Basilico, C.2
  • 4
    • 0035929239 scopus 로고    scopus 로고
    • Structural basis for SRY-dependent 46-X,Y sex reversal: Modulation of DNA bending by a naturally occurring point mutation
    • DOI 10.1006/jmbi.2001.4977
    • Murphy, E. C., Zhurkin, V. B., Louis, J. M., Cornilescu, G., and Clore, G. M. (2001) Structural basis for SRY-dependent 46-X,Y sex reversal: modulation of DNA bending by a naturally occurring point mutation. J. Mol. Biol. 312, 481-499 (Pubitemid 32928119)
    • (2001) Journal of Molecular Biology , vol.312 , Issue.3 , pp. 481-499
    • Murphy, E.C.1    Zhurkin, V.B.2    Louis, J.M.3    Cornilescu, G.4    Clore, G.M.5
  • 5
    • 0028200262 scopus 로고
    • Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules
    • DOI 10.1016/0092-8674(94)90231-3
    • Klemm, J. D., Rould, M. A., Aurora, R., Herr, W., and Pabo, C. O. (1994) Crystal structure of the Oct1 POU domain bound to an octamer site: DNA recognition with tethered DNA-binding modules. Cell 77, 21-32 (Pubitemid 24184684)
    • (1994) Cell , vol.77 , Issue.1 , pp. 21-32
    • Klemm, J.D.1    Rould, M.A.2    Aurora, R.3    Herr, W.4    Pabo, C.O.5
  • 6
    • 0034791092 scopus 로고    scopus 로고
    • Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping
    • DOI 10.1016/S1097-2765(01)00336-7
    • Reményi, A., Tomilin, A., Pohl, E., Lins, K., Philippsen, A., Reinbold, R., Schöler, H. R., and Wilmanns, M. (2001) Differential dimer activities of the transcription factor Oct1 by DNA-induced interface swapping. Mol. Cell 8, 569-580 (Pubitemid 32946934)
    • (2001) Molecular Cell , vol.8 , Issue.3 , pp. 569-580
    • Remenyi, A.1    Tomilin, A.2    Pohl, E.3    Lins, K.4    Philippsen, A.5    Reinbold, R.6    Scholer, H.R.7    Wilmanns, M.8
  • 7
    • 0346462991 scopus 로고    scopus 로고
    • Molecular Basis for Synergistic Transcriptional Activation by Oct1 and Sox2 Revealed from the Solution Structure of the 42-kDa Oct1·Sox2· Hoxb1-DNA Ternary Transcription Factor Complex
    • DOI 10.1074/jbc.M309790200
    • Williams, D. C., Jr., Cai, M., and Clore, G. M. (2004) Molecular basis for synergistic transcriptional activation by Oct1 and Sox2 revealed from the solution structure of the 42-kDa Oct1·Sox2·Hoxb1-DNA ternary transcription factor complex. J. Biol. Chem. 279, 1449-1457 (Pubitemid 38082673)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.2 , pp. 1449-1457
    • Williams Jr., D.C.1    Cai, M.2    Clore, G.M.3
  • 8
    • 0042161878 scopus 로고    scopus 로고
    • Crystal structure of a POU/HMG/DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers
    • DOI 10.1101/gad.269303
    • Reményi, A., Lins, K., Nissen, L. J., Reinbold, R., Schöler, H. R., and Wilmanns, M. (2003) Crystal structure of a POU·HMG·DNA ternary complex suggests differential assembly of Oct4 and Sox2 on two enhancers. Genes Dev. 17, 2048-2059 (Pubitemid 36999330)
    • (2003) Genes and Development , vol.17 , Issue.16 , pp. 2048-2059
    • Remenyi, A.1    Lins, K.2    Nissen, L.J.3    Reinbold, R.4    Scholer, H.R.5    Wilmanns, M.6
  • 10
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • von Hippel, P. H., and Berg, O. G. (1989) Facilitated target location in biological systems. J. Biol. Chem. 264, 675-678
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • Von Hippel, P.H.1    Berg, O.G.2
  • 11
    • 3042579602 scopus 로고    scopus 로고
    • How do site-specific DNA-binding proteins find their targets?
    • DOI 10.1093/nar/gkh624
    • Halford, S. E., and Marko, J. F. (2004) How do site-specific DNA-binding proteins find their targets? Nucleic Acids Res. 32, 3040-3052 (Pubitemid 39022995)
    • (2004) Nucleic Acids Research , vol.32 , Issue.10 , pp. 3040-3052
    • Halford, S.E.1    Marko, J.F.2
  • 12
    • 70349093561 scopus 로고    scopus 로고
    • Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low population states of biological macromolecules and their complexes
    • Clore, G. M., and Iwahara, J. (2009) Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low population states of biological macromolecules and their complexes. Chem. Rev. 109, 4108-4139
    • (2009) Chem. Rev. , vol.109 , pp. 4108-4139
    • Clore, G.M.1    Iwahara, J.2
  • 13
    • 79251586250 scopus 로고    scopus 로고
    • Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation
    • Clore, G. M. (2011) Exploring sparsely populated states of macromolecules by diamagnetic and paramagnetic NMR relaxation. Protein Sci. 20, 229-246
    • (2011) Protein Sci. , vol.20 , pp. 229-246
    • Clore, G.M.1
  • 15
    • 33646356250 scopus 로고    scopus 로고
    • Detecting transient intermediates in macromolecular binding by paramagnetic NMR
    • Iwahara, J., and Clore, G. M. (2006) Detecting transient intermediates in macromolecular binding by paramagnetic NMR. Nature 440, 1227-1230
    • (2006) Nature , vol.440 , pp. 1227-1230
    • Iwahara, J.1    Clore, G.M.2
  • 17
    • 79959360942 scopus 로고    scopus 로고
    • Intra- and intermolecular translocation of the bidomain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR
    • Takayama, Y., and Clore, G. M. (2011) Intra- and intermolecular translocation of the bidomain transcription factor Oct1 characterized by liquid crystal and paramagnetic NMR. Proc. Natl. Acad. Sci. U.S.A. 108, E169-E176
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108
    • Takayama, Y.1    Clore, G.M.2
  • 18
    • 84860359548 scopus 로고    scopus 로고
    • Interplay between minor and major groove-binding transcription factors Sox2 and Oct1 in translocation on DNA studied by paramagnetic and diamagnetic NMR
    • Takayama, Y., and Clore, G. M. (2012) Interplay between minor and major groove-binding transcription factors Sox2 and Oct1 in translocation on DNA studied by paramagnetic and diamagnetic NMR. J. Biol. Chem. 287, 14349-14363
    • (2012) J. Biol. Chem. , vol.287 , pp. 14349-14363
    • Takayama, Y.1    Clore, G.M.2
  • 19
    • 80755172250 scopus 로고    scopus 로고
    • Exploring translocation of proteins on DNA by NMR
    • Clore, G. M. (2011) Exploring translocation of proteins on DNA by NMR. J. Biomol. NMR 51, 209-219
    • (2011) J. Biomol. NMR , vol.51 , pp. 209-219
    • Clore, G.M.1
  • 20
    • 31544448614 scopus 로고    scopus 로고
    • Direct observation of enhanced translocation of a homeodomain between DNA cognate sites by NMR exchange spectroscopy
    • DOI 10.1021/ja056786o
    • Iwahara, J., and Clore, G. M. (2006) Direct observation of enhanced translocation of a homeodomain between DNA cognate sites by NMR exchange spectroscopy. J. Am. Chem. Soc. 128, 404-405 (Pubitemid 43157521)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.2 , pp. 404-405
    • Iwahara, J.1    Clore, G.M.2
  • 21
    • 52949100201 scopus 로고    scopus 로고
    • Global jumping and domain-specific intersegment transfer between DNA cognate sites of the multidomain transcription factor Oct1
    • Doucleff, M., and Clore, G. M. (2008) Global jumping and domain-specific intersegment transfer between DNA cognate sites of the multidomain transcription factor Oct1. Proc. Natl. Acad. Sci. U.S.A. 105, 13871-13876
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13871-13876
    • Doucleff, M.1    Clore, G.M.2
  • 22
    • 0030820931 scopus 로고    scopus 로고
    • Synergistic activation of the fibroblast growth factor 4 enhancer by Sox2 and Oct-3 depends on protein-protein interactions facilitated by a specific spatial arrangement of factor binding sites
    • Ambrosetti, D. C., Basilico, C., and Dailey, L. (1997) Synergistic activation of the fibroblast growth factor 4 enhancer by Sox2 and Oct3 depends on protein/protein interactions facilitated by a specific spatial arrangement of factor binding sites. Mol. Cell Biol. 17, 6321-6329 (Pubitemid 27451176)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.11 , pp. 6321-6329
    • Ambrosetti, D.-C.1    Basilico, C.2    Dailey, L.3
  • 23
    • 0035827568 scopus 로고    scopus 로고
    • The recruitment of SOX·OCT complexes and the differential activity of HOXA1 and HOXB1 modulate the Hoxb1 auto-regulatory enhancer function
    • Di Rocco, G., Gavalas, A., Popperl, H., Krumlauf, R., Mavilio, F., and Zappavigna, V. (2001) The recruitment of SOX·OCT complexes and the differential activity of HOXA1 and HOXB1 modulate the Hoxb1 auto-regulatory enhancer function. J. Biol. Chem. 276, 20506-20515
    • (2001) J. Biol. Chem. , vol.276 , pp. 20506-20515
    • Di Rocco, G.1    Gavalas, A.2    Popperl, H.3    Krumlauf, R.4    Mavilio, F.5    Zappavigna, V.6
  • 24
    • 0037533875 scopus 로고    scopus 로고
    • EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement
    • DOI 10.1021/ja034488q
    • Iwahara, J., Anderson, D. E., Murphy, E. C., and Clore, G. M. (2003) EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement. J. Am. Chem. Soc. 125, 6634-6635 (Pubitemid 36667439)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.22 , pp. 6634-6635
    • Iwahara, J.1    Anderson, D.E.2    Murphy, E.C.3    Clore, G.M.4
  • 25
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 26
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A., and Blevins, R. A. (1994) NMR View: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 27
    • 35848970780 scopus 로고    scopus 로고
    • TROSY-based z-exchange spectroscopy: Application to the determination of the activation energy for intermolecular protein translocation between specific sites on different DNA molecules
    • DOI 10.1021/ja074604f
    • Sahu, D., Clore, G. M., and Iwahara, J. (2007) TROSY-based z-exchange spectroscopy: application to the determination of the activation energy for intermolecular protein translocation between specific sites on different DNA molecules. J. Am. Chem. Soc. 129, 13232-13237 (Pubitemid 350058364)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.43 , pp. 13232-13237
    • Sahu, D.1    Clore, G.M.2    Iwahara, J.3
  • 28
    • 33845182844 scopus 로고
    • Two-dimensional chemical exchange NMR spectroscopy by proton-detected heteronuclear correlation
    • Montelione, G. T., and Wagner, G. (1989) Two-dimensional chemical exchange NMR spectroscopy by proton-detected heteronuclear correlation. J. Am. Chem. Soc. 111, 3096-3098
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 3096-3098
    • Montelione, G.T.1    Wagner, G.2
  • 29
    • 0001304511 scopus 로고
    • Application of two-dimensional NMR to kinetics of chemical exchange
    • Perrin, C. L., and Dwyer, T. J. (1990) Application of two-dimensional NMR to kinetics of chemical exchange. Chem. Rev. 90, 935-967
    • (1990) Chem. Rev. , vol.90 , pp. 935-967
    • Perrin, C.L.1    Dwyer, T.J.2
  • 31
    • 0010957050 scopus 로고
    • Reaction rates by nuclear magnetic resonance
    • McConnell, H. M. (1958) Reaction rates by nuclear magnetic resonance. J. Chem. Phys. 28, 430-431
    • (1958) J. Chem. Phys. , vol.28 , pp. 430-431
    • McConnell, H.M.1
  • 32
    • 0032557503 scopus 로고    scopus 로고
    • Electrostatic enhancement of diffusion-controlled protein-protein association: Comparison of theory and experiment on barnase and barstar
    • DOI 10.1006/jmbi.1998.1747
    • Vijayakumar, M., Wong, K. Y., Schreiber, G., Fersht, A. R., Szabo, A., and Zhou, H. X. (1998) Electrostatic enhancement of diffusion-controlled protein/protein association: comparison of theory and experiment on barnase and barstar. J. Mol. Biol. 278, 1015-1024 (Pubitemid 28239701)
    • (1998) Journal of Molecular Biology , vol.278 , Issue.5 , pp. 1015-1024
    • Vijayakumar, M.1    Wong, K.-Y.2    Schreiber, G.3    Fersht, A.R.4    Szabo, A.5    Zhou, H.-X.6
  • 33
    • 19744381543 scopus 로고    scopus 로고
    • Enhancement of association rates by nonspecific binding to DNA and cell membranes
    • Zhou, H. X., and Szabo, A. (2004) Enhancement of association rates by nonspecific binding to DNA and cell membranes. Phys. Rev. Lett. 93, 178101
    • (2004) Phys. Rev. Lett. , vol.93 , pp. 178101
    • Zhou, H.X.1    Szabo, A.2
  • 34
    • 84864280124 scopus 로고    scopus 로고
    • Sex-determining region Y-box 2 expression predicts poor prognosis in human ovarian carcinoma
    • March 9, 10.1016/j.humpath.2011.10.016
    • Zhang, J., Chang, D. Y., Mercado-Uribe, I., and Liu, J. (March 9, 2012) Sex-determining region Y-box 2 expression predicts poor prognosis in human ovarian carcinoma. Hum. Pathol. 10.1016/j.humpath.2011.10.016
    • (2012) Hum. Pathol.
    • Zhang, J.1    Chang, D.Y.2    Mercado-Uribe, I.3    Liu, J.4
  • 35
    • 70349338871 scopus 로고    scopus 로고
    • Stem cells, stress, metabolism, and cancer: A drama in two Octs
    • Kang, J., Shakya, A., and Tantin, D. (2009) Stem cells, stress, metabolism, and cancer: a drama in two Octs. Trends Biochem. Sci. 34, 491-499
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 491-499
    • Kang, J.1    Shakya, A.2    Tantin, D.3
  • 37


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.