메뉴 건너뛰기




Volumn 47, Issue 1, 2008, Pages 30-39

Basic folded and low-populated locally disordered conformers of SUMO-2 characterized by NMR spectroscopy at varying pressures

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMERS; FOLDED STATE; NEDD8; UBIQUITIN;

EID: 37849000182     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7014458     Document Type: Article
Times cited : (12)

References (44)
  • 2
    • 29144518532 scopus 로고    scopus 로고
    • The ubiquitin domain superfold: Structure-based sequence alignments and characterization of binding epitopes
    • Kiel, C., and Serrano, L. (2006) The ubiquitin domain superfold: Structure-based sequence alignments and characterization of binding epitopes, J. Mol. Biol 355, 821-844.
    • (2006) J. Mol. Biol , vol.355 , pp. 821-844
    • Kiel, C.1    Serrano, L.2
  • 3
    • 0034253588 scopus 로고    scopus 로고
    • Evolution and function of ubiquitin-like protein-conugation systems
    • Hochstrasser, M. (2000) Evolution and function of ubiquitin-like protein-conugation systems, Nat. Cell Biol. 2, E153-E157.
    • (2000) Nat. Cell Biol , vol.2
    • Hochstrasser, M.1
  • 4
    • 0035969236 scopus 로고    scopus 로고
    • The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice
    • Tateishi, K., Omata, M., Tanaka, K., and Chiba, T. (2001) The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice, J. Biol. Chem. 155, 571-579.
    • (2001) J. Biol. Chem , vol.155 , pp. 571-579
    • Tateishi, K.1    Omata, M.2    Tanaka, K.3    Chiba, T.4
  • 5
    • 0034523266 scopus 로고    scopus 로고
    • SUMO-Nonclassical ubiquitin
    • Melchior, F. (2000) SUMO-Nonclassical ubiquitin, Annu. Rev. Cell Dev. Biol. 16, 591-626.
    • (2000) Annu. Rev. Cell Dev. Biol , vol.16 , pp. 591-626
    • Melchior, F.1
  • 6
    • 0035336677 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Hay, R. T. (2001) Protein modification by SUMO, Trends Biochem. Sci. 26, 332-333.
    • (2001) Trends Biochem. Sci , vol.26 , pp. 332-333
    • Hay, R.T.1
  • 8
    • 1342279419 scopus 로고    scopus 로고
    • SUMO modification of proteins other than transcription factors
    • Watts, F. Z. (2004) SUMO modification of proteins other than transcription factors, Cell Dev. Biol. 15, 211-220.
    • (2004) Cell Dev. Biol , vol.15 , pp. 211-220
    • Watts, F.Z.1
  • 9
    • 33745156511 scopus 로고    scopus 로고
    • Ubiquitin and SUMO systems in the reguration of mitotic checkpoints
    • Gutierrez, G. J., and Ronai, Z. (2006) Ubiquitin and SUMO systems in the reguration of mitotic checkpoints, Trends Biochem. Sci. 31, 324-332.
    • (2006) Trends Biochem. Sci , vol.31 , pp. 324-332
    • Gutierrez, G.J.1    Ronai, Z.2
  • 10
    • 3042644131 scopus 로고    scopus 로고
    • A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptability to type I diabetes mellitus
    • Bohren, K. M., Nadkarni, V., Song, J. H., Gabbay, K. H., and Owerbach, D. (2004) A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptability to type I diabetes mellitus, J. Biol. Chem. 279, 27233-27238.
    • (2004) J. Biol. Chem , vol.279 , pp. 27233-27238
    • Bohren, K.M.1    Nadkarni, V.2    Song, J.H.3    Gabbay, K.H.4    Owerbach, D.5
  • 12
    • 14344261035 scopus 로고    scopus 로고
    • Solution structure of human SUMO-3 C47S and its binding surface for UBC9
    • Ding, H., Xu, Y., Chen, Q., Dai, H., Tang, Y., Wu, J., and Shi, Y. (2005) Solution structure of human SUMO-3 C47S and its binding surface for UBC9, Biochemistry 44, 2790-2799.
    • (2005) Biochemistry , vol.44 , pp. 2790-2799
    • Ding, H.1    Xu, Y.2    Chen, Q.3    Dai, H.4    Tang, Y.5    Wu, J.6    Shi, Y.7
  • 13
    • 7044269671 scopus 로고    scopus 로고
    • Crystal structures of the human SUMO-2 protein at 1.6 Å and 1.2 Å resolution: Implication on the functional differences of SUMO proteins
    • Huang, W. C., Ko, T. P., Li, S. S. L., and Wang, A. H.-J. (2004) Crystal structures of the human SUMO-2 protein at 1.6 Å and 1.2 Å resolution: Implication on the functional differences of SUMO proteins, Eur. J. Biochem. 271, 4114-4122.
    • (2004) Eur. J. Biochem , vol.271 , pp. 4114-4122
    • Huang, W.C.1    Ko, T.P.2    Li, S.S.L.3    Wang, A.H.-J.4
  • 14
    • 0035856546 scopus 로고    scopus 로고
    • Two folded conformers of ubiquitin revealed by high-pressure NMR
    • Kitahara, R., Yamada, H., and Akasaka, K. (2001) Two folded conformers of ubiquitin revealed by high-pressure NMR, Biochemistry 40, 13556-13563.
    • (2001) Biochemistry , vol.40 , pp. 13556-13563
    • Kitahara, R.1    Yamada, H.2    Akasaka, K.3
  • 15
    • 0037452877 scopus 로고    scopus 로고
    • Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding
    • Kitahara, R., and Akasaka, K. (2003) Close identity of a pressure-stabilized intermediate with a kinetic intermediate in protein folding, Proc. Natl. Acad. Sci. U.S.A. 100, 3167-3172.
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 3167-3172
    • Kitahara, R.1    Akasaka, K.2
  • 16
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar
    • Kitahara, R., Yokoyama, S., and Akasaka, K. (2005) NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar, J. Mol. Biol. 347, 277-285.
    • (2005) J. Mol. Biol , vol.347 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 18
    • 0032923295 scopus 로고    scopus 로고
    • Cell-free production and stable-isotope labeling of milligram quantities of proteins
    • Kigawa, T., Yabuki, T., Yoshida, Y., Tsutsui, M., Ito, Y., Shibata, T., and Yokoyama, S. (1999) Cell-free production and stable-isotope labeling of milligram quantities of proteins, FEBS Lett. 442, 15-19.
    • (1999) FEBS Lett , vol.442 , pp. 15-19
    • Kigawa, T.1    Yabuki, T.2    Yoshida, Y.3    Tsutsui, M.4    Ito, Y.5    Shibata, T.6    Yokoyama, S.7
  • 22
    • 0025341339 scopus 로고
    • 15N spectra of proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin
    • 15N spectra of proteins: Heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin, Biochemistry 29, 4659-4667.
    • (1990) Biochemistry , vol.29 , pp. 4659-4667
    • Ikura, M.1    Kay, L.E.2    Bax, A.3
  • 23
    • 0028019827 scopus 로고
    • Multidimensional nuclear magnetic resonance methods for protein studies
    • Bax, A. (1994) Multidimensional nuclear magnetic resonance methods for protein studies, Curr. Opin. Struct. Biol. 4, 738-744.
    • (1994) Curr. Opin. Struct. Biol , vol.4 , pp. 738-744
    • Bax, A.1
  • 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
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A., and Blevins, R. A. (1994) NMRView: 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
    • 34547923673 scopus 로고    scopus 로고
    • KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies
    • Kobayashi, N., Iwahara, J., Koshiba, S., Tomizawa, T., Tochio, N., Guntert, P., Kigawa, T., and Yokoyama, S. (2007) KUJIRA, a package of integrated modules for systematic and interactive analysis of NMR data directed to high-throughput NMR structure studies, J. Biomol. NMR 39, 31-52.
    • (2007) J. Biomol. NMR , vol.39 , pp. 31-52
    • Kobayashi, N.1    Iwahara, J.2    Koshiba, S.3    Tomizawa, T.4    Tochio, N.5    Guntert, P.6    Kigawa, T.7    Yokoyama, S.8
  • 29
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology, J. Biomol. NMR 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 30
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA, J. Mol. Biol. 273, 283-298.
    • (1997) J. Mol. Biol , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 31
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmann, J. A., MacArthur, M. W., Kaptain, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR, J. Biomol. NMR 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.2    MacArthur, M.W.3    Kaptain, R.4    Thornton, J.M.5
  • 32
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 33
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., Güntert, P., and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA, J. Mol. Biol. 319, 209-227.
    • (2002) J. Mol. Biol , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 34
    • 0034912667 scopus 로고    scopus 로고
    • Akasaka, K., and Yamada, H. (2001) On-Line Cell High Pressure Nuclear Magnetic Resonance Technique: Application to Protein Studies, in Methods in Enzymology, 338: Nuclear Magnetic Resonance of Biological Macromolecules, Part A (James, T. L., et al., Eds.) pp 134-158, Academic Press, New York.
    • Akasaka, K., and Yamada, H. (2001) On-Line Cell High Pressure Nuclear Magnetic Resonance Technique: Application to Protein Studies, in Methods in Enzymology, Volume 338: Nuclear Magnetic Resonance of Biological Macromolecules, Part A (James, T. L., et al., Eds.) pp 134-158, Academic Press, New York.
  • 35
    • 33646900712 scopus 로고    scopus 로고
    • Probing conformational fluctuation of proteins by pressure perturbation
    • Akasaka, K. (2006) Probing conformational fluctuation of proteins by pressure perturbation, Chem. Rev. 106, 1814-1835.
    • (2006) Chem. Rev , vol.106 , pp. 1814-1835
    • Akasaka, K.1
  • 36
    • 0035247443 scopus 로고    scopus 로고
    • Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields
    • Yamada, H., Nishikawa, K., Honda, M., Shimura, T., Tabayashi, K., and Akasaka, K. (2001) Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields, Rev. Sci. Instrum. 72, 1463-1471.
    • (2001) Rev. Sci. Instrum , vol.72 , pp. 1463-1471
    • Yamada, H.1    Nishikawa, K.2    Honda, M.3    Shimura, T.4    Tabayashi, K.5    Akasaka, K.6
  • 37
    • 33947100840 scopus 로고    scopus 로고
    • NMR characterization of the energy landscape of SUMO-1 in the native-state ensemble
    • Kumar, A., Srivastava, S., and Hosur, R. V. (2007) NMR characterization of the energy landscape of SUMO-1 in the native-state ensemble, J. Mol. Biol. 367, 1480-1493.
    • (2007) J. Mol. Biol , vol.367 , pp. 1480-1493
    • Kumar, A.1    Srivastava, S.2    Hosur, R.V.3
  • 39
    • 0347416977 scopus 로고    scopus 로고
    • The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an El
    • Walden, H., Podgorski, M. S., Huang, D. T., Miller, D. W., Howard, R. J., Minor, D. L., Jr., Holton, J. M., and Shulman, B. A. (2003) The structure of the APPBP1-UBA3-NEDD8-ATP complex reveals the basis for selective ubiquitin-like protein activation by an El, Mol. Cell 12, 1427-1437.
    • (2003) Mol. Cell , vol.12 , pp. 1427-1437
    • Walden, H.1    Podgorski, M.S.2    Huang, D.T.3    Miller, D.W.4    Howard, R.J.5    Minor Jr., D.L.6    Holton, J.M.7    Shulman, B.A.8
  • 40
    • 0033516511 scopus 로고    scopus 로고
    • Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution
    • Miura, T., Klaus, W., Gsell, B., Miyamoto, C., and Senn, H. (1999) Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution, J. Mol. Biol. 290, 213-228.
    • (1999) J. Mol. Biol , vol.290 , pp. 213-228
    • Miura, T.1    Klaus, W.2    Gsell, B.3    Miyamoto, C.4    Senn, H.5
  • 42
    • 34548433080 scopus 로고    scopus 로고
    • Theoretical study of the partial molar volume change associated with the pressure-induced structural transition of ubiquitin
    • Imai, T., Ohyama, S., Kovalenko, A., and Hirata, F. (2007) Theoretical study of the partial molar volume change associated with the pressure-induced structural transition of ubiquitin, Protein Sci. 16, 1927-1933.
    • (2007) Protein Sci , vol.16 , pp. 1927-1933
    • Imai, T.1    Ohyama, S.2    Kovalenko, A.3    Hirata, F.4
  • 43
    • 0033594989 scopus 로고    scopus 로고
    • Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability
    • Ibara-Molero, B., Loladze, V. V., Makhatadze, G. I., and Sanchez-Ruiz, J. M. (1999) Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability, Biochemistry 38, 8138-8149.
    • (1999) Biochemistry , vol.38 , pp. 8138-8149
    • Ibara-Molero, B.1    Loladze, V.V.2    Makhatadze, G.I.3    Sanchez-Ruiz, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.