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Volumn 287, Issue 34, 2012, Pages 28349-28361

The structure of vimentin linker 1 and rod 1B domains characterized by site-directed spin-labeling electron paramagnetic resonance (SDSL-EPR) and X-ray crystallography

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL STRUCTURES; COILED COIL; CRYSTALLOGRAPHIC DATA; ELECTRON PARAMAGNETIC RESONANCE SPECTRUM; FLEXIBLE SEGMENTS; INTERMEDIATE FILAMENTS; LOCAL DISTORTION; PRIMARY SEQUENCES; SPECTRAL DATA; SPIN LABEL; STRUCTURAL MODELS; TETRAMERS; VIMENTIN;

EID: 84865204718     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.334011     Document Type: Article
Times cited : (49)

References (47)
  • 1
    • 0022172443 scopus 로고
    • Intermediate filaments. Conformity and diversity of expression and structure
    • Steinert, P. M., and Parry, D. A. (1985) Intermediate filaments. Conformity and diversity of expression and structure. Annu. Rev. Cell Biol. 1, 41-65
    • (1985) Annu. Rev. Cell Biol. , vol.1 , pp. 41-65
    • Steinert, P.M.1    Parry, D.A.2
  • 3
    • 0017118068 scopus 로고
    • Bovine epidermal keratin filament assembly in vitro
    • Steinert, P. M., and Gullino, M. I. (1976) Bovine epidermal keratin filament assembly in vitro. Biochem. Biophys. Res. Commun. 70, 221-227
    • (1976) Biochem. Biophys. Res. Commun. , vol.70 , pp. 221-227
    • Steinert, P.M.1    Gullino, M.I.2
  • 4
    • 0019888143 scopus 로고
    • Reconstitution of intermediate-sized filaments from denatured monomeric vimentin
    • Renner, W., Franke, W. W., Schmid, E., Geisler, N., Weber, K., and Mandelkow, E. (1981) Reconstitution of intermediate-sized filaments from denatured monomeric vimentin. J. Mol. Biol. 149, 285-306
    • (1981) J. Mol. Biol. , vol.149 , pp. 285-306
    • Renner, W.1    Franke, W.W.2    Schmid, E.3    Geisler, N.4    Weber, K.5    Mandelkow, E.6
  • 6
    • 33747364924 scopus 로고    scopus 로고
    • Crystal structure of polymerization-competent actin
    • Klenchin, V. A., Khaitlina, S. Y., and Rayment, I. (2006) Crystal structure of polymerization-competent actin. J. Mol. Biol. 362, 140-150
    • (2006) J. Mol. Biol. , vol.362 , pp. 140-150
    • Klenchin, V.A.1    Khaitlina, S.Y.2    Rayment, I.3
  • 7
    • 0035834521 scopus 로고    scopus 로고
    • Refined structure of α β-tubulin at 3.5 Å resolution
    • Löwe, J., Li, H., Downing, K. H., and Nogales, E. (2001) Refined structure of α β-tubulin at 3.5 Å resolution. J. Mol. Biol. 313, 1045-1057
    • (2001) J. Mol. Biol. , vol.313 , pp. 1045-1057
    • Löwe, J.1    Li, H.2    Downing, K.H.3    Nogales, E.4
  • 8
    • 0020446742 scopus 로고
    • The cDNA sequence of a human epidermal keratin. Divergence of sequence but conservation of structure among intermediate filament proteins
    • Hanukoglu, I., and Fuchs, E. (1982) The cDNA sequence of a human epidermal keratin. Divergence of sequence but conservation of structure among intermediate filament proteins. Cell 31, 243-252
    • (1982) Cell , vol.31 , pp. 243-252
    • Hanukoglu, I.1    Fuchs, E.2
  • 9
    • 0020614212 scopus 로고
    • The cDNA sequence of a Type II cytoskeletal keratin reveals constant and variable structural domains among keratins
    • Hanukoglu, I., and Fuchs, E. (1983) The cDNA sequence of a Type II cytoskeletal keratin reveals constant and variable structural domains among keratins. Cell 33, 915-924
    • (1983) Cell , vol.33 , pp. 915-924
    • Hanukoglu, I.1    Fuchs, E.2
  • 10
    • 0020338526 scopus 로고
    • The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins
    • Geisler, N., and Weber, K. (1982) The amino acid sequence of chicken muscle desmin provides a common structural model for intermediate filament proteins. EMBO J. 1, 1649-1656
    • (1982) EMBO J. , vol.1 , pp. 1649-1656
    • Geisler, N.1    Weber, K.2
  • 11
    • 0000920828 scopus 로고
    • The Packing of α-helices. Simple coiled-coils
    • Crick, F. H. C. (1953) The Packing of α-helices. Simple coiled-coils. Acta Crystallogr. 6, 689-697
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 12
    • 0022312879 scopus 로고
    • The molecular biology of intermediate filaments
    • Steinert, P. M., Steven, A. C., and Roop, D. R. (1985) The molecular biology of intermediate filaments. Cell 42, 411-420
    • (1985) Cell , vol.42 , pp. 411-420
    • Steinert, P.M.1    Steven, A.C.2    Roop, D.R.3
  • 13
    • 0022272929 scopus 로고
    • Intermediate filaments. Structural conservation and divergence
    • Weber, K., and Geisler, N. (1985) Intermediate filaments. Structural conservation and divergence. Ann. N.Y. Acad. Sci. 455, 126-143
    • (1985) Ann. N.Y. Acad. Sci. , vol.455 , pp. 126-143
    • Weber, K.1    Geisler, N.2
  • 14
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments. Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • Herrmann, H., and Aebi, U. (2004) Intermediate filaments. Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds. Annu. Rev. Biochem. 73, 749-789
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 15
    • 0033498452 scopus 로고    scopus 로고
    • Intermediate filaments. Molecular architecture, assembly, dynamics, and polymorphism
    • Parry, D. A., and Steinert, P. M. (1999) Intermediate filaments. Molecular architecture, assembly, dynamics, and polymorphism. Q. Rev. Biophys. 32, 99-187
    • (1999) Q. Rev. Biophys. , vol.32 , pp. 99-187
    • Parry, D.A.1    Steinert, P.M.2
  • 16
    • 0026545645 scopus 로고
    • A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering
    • Lane, E. B., Rugg, E. L., Navsaria, H., Leigh, I. M., Heagerty, A. H., Ishida-Yamamoto, A., and Eady, R. A. (1992) A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering. Nature 356, 244-246
    • (1992) Nature , vol.356 , pp. 244-246
    • Lane, E.B.1    Rugg, E.L.2    Navsaria, H.3    Leigh, I.M.4    Heagerty, A.H.5    Ishida-Yamamoto, A.6    Eady, R.A.7
  • 17
    • 0001608503 scopus 로고
    • Primary and secondary structure of if protein chains and modes of molecular aggregatin
    • (Goldman, R. D., and Steinert, P. M., eds) Plenum, New York
    • Parry, D. (1990) Primary and secondary structure of IF protein chains and modes of molecular aggregatin. in Cellular and molecular biology of intermediate filaments (Goldman, R. D., and Steinert, P. M., eds) pp. 175-204, Plenum, New York
    • (1990) Cellular and Molecular Biology of Intermediate Filaments , pp. 175-204
    • Parry, D.1
  • 18
    • 77952059501 scopus 로고    scopus 로고
    • Site-directed spin labeling and electron paramagnetic resonance determination of vimentin head domain structure
    • Aziz, A., Hess, J. F., Budamagunta, M. S., Voss, J. C., and Fitzgerald, P. G. (2010) Site-directed spin labeling and electron paramagnetic resonance determination of vimentin head domain structure. J. Biol. Chem. 285, 15278-15285
    • (2010) J. Biol. Chem. , vol.285 , pp. 15278-15285
    • Aziz, A.1    Hess, J.F.2    Budamagunta, M.S.3    Voss, J.C.4    Fitzgerald, P.G.5
  • 21
    • 33749364090 scopus 로고    scopus 로고
    • Characterization of the linker 2 region in human vimentin using site-directed spin labeling and electron paramagnetic resonance
    • Hess, J. F., Budamagunta, M. S., Shipman, R. L., FitzGerald, P. G., and Voss, J. C. (2006) Characterization of the linker 2 region in human vimentin using site-directed spin labeling and electron paramagnetic resonance. Biochemistry 45, 11737-11743
    • (2006) Biochemistry , vol.45 , pp. 11737-11743
    • Hess, J.F.1    Budamagunta, M.S.2    Shipman, R.L.3    FitzGerald, P.G.4    Voss, J.C.5
  • 24
    • 0037086445 scopus 로고    scopus 로고
    • Conserved segments 1A and 2B of the intermediate filament dimer. Their atomic structures and role in filament assembly
    • Strelkov, S. V., Herrmann, H., Geisler, N., Wedig, T., Zimbelmann, R., Aebi, U., and Burkhard, P. (2002) Conserved segments 1A and 2B of the intermediate filament dimer. Their atomic structures and role in filament assembly. EMBO J. 21, 1255-1266
    • (2002) EMBO J. , vol.21 , pp. 1255-1266
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Wedig, T.4    Zimbelmann, R.5    Aebi, U.6    Burkhard, P.7
  • 26
    • 33747768593 scopus 로고    scopus 로고
    • Hendecad repeat in segment 2A and linker L2 of intermediate filament chains implies the possibility of a right-handed coiled-coil structure
    • Parry, D. A. (2006) Hendecad repeat in segment 2A and linker L2 of intermediate filament chains implies the possibility of a right-handed coiled-coil structure. J. Struct. Biol. 155, 370-374
    • (2006) J. Struct. Biol. , vol.155 , pp. 370-374
    • Parry, D.A.1
  • 27
    • 65449188330 scopus 로고    scopus 로고
    • Head and rod 1 interactions in vimentin. Identification of contact sites, structure, and changes with phosphorylation using site-directed spin labeling and electron paramagnetic resonance
    • Aziz, A., Hess, J. F., Budamagunta, M. S., FitzGerald, P. G., and Voss, J. C. (2009) Head and rod 1 interactions in vimentin. Identification of contact sites, structure, and changes with phosphorylation using site-directed spin labeling and electron paramagnetic resonance. J. Biol. Chem. 284, 7330-7338
    • (2009) J. Biol. Chem. , vol.284 , pp. 7330-7338
    • Aziz, A.1    Hess, J.F.2    Budamagunta, M.S.3    FitzGerald, P.G.4    Voss, J.C.5
  • 28
    • 7244221578 scopus 로고    scopus 로고
    • Structural characterization of human vimentin rod 1 and the sequencing of assembly steps in intermediate filament formation in vitro using site-directed spin labeling and electron paramagnetic resonance
    • Hess, J. F., Budamagunta, M. S., Voss, J. C., and FitzGerald, P. G. (2004) Structural characterization of human vimentin rod 1 and the sequencing of assembly steps in intermediate filament formation in vitro using site-directed spin labeling and electron paramagnetic resonance. J. Biol. Chem. 279, 44841-44846
    • (2004) J. Biol. Chem. , vol.279 , pp. 44841-44846
    • Hess, J.F.1    Budamagunta, M.S.2    Voss, J.C.3    FitzGerald, P.G.4
  • 29
    • 33749357063 scopus 로고
    • Intermediate filament structure. 3. Analysis of sequence homologies
    • Conway, J. F., and Parry, D. A. D. (1988) Intermediate filament structure. 3. Analysis of sequence homologies. Int. J. Biol. Macromol. 10, 79-98
    • (1988) Int. J. Biol. Macromol. , vol.10 , pp. 79-98
    • Conway, J.F.1    Parry, D.A.D.2
  • 30
    • 55049132861 scopus 로고    scopus 로고
    • Targeting the human cancer pathway protein interaction network by structural genomics
    • Huang, Y. J., Hang, D., Lu, L. J., Tong, L., Gerstein, M. B., and Montelione, G. T. (2008) Targeting the human cancer pathway protein interaction network by structural genomics. Mol. Cell Proteomics 7, 2048-2060
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 2048-2060
    • Huang, Y.J.1    Hang, D.2    Lu, L.J.3    Tong, L.4    Gerstein, M.B.5    Montelione, G.T.6
  • 32
    • 0037394492 scopus 로고    scopus 로고
    • A deliberate approach to screening for initial crystallization conditions of biological macromolecules
    • Luft, J. R., Collins, R. J., Fehrman, N. A., Lauricella, A. M., Veatch, C. K., and DeTitta, G. T. (2003) A deliberate approach to screening for initial crystallization conditions of biological macromolecules. J. Struct. Biol. 142, 170-179
    • (2003) J. Struct. Biol. , vol.142 , pp. 170-179
    • Luft, J.R.1    Collins, R.J.2    Fehrman, N.A.3    Lauricella, A.M.4    Veatch, C.K.5    DeTitta, G.T.6
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
  • 36
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N., and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement. Acta Crystallogr. D Biol. Crystallogr. 57, 122-133
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 37
    • 0033994775 scopus 로고    scopus 로고
    • HELANAL.Aprogram to characterize helix geometry in proteins
    • Bansal, M., Kumar, S., and Velavan, R. (2000) HELANAL.Aprogram to characterize helix geometry in proteins. J. Biomol. Struct. Dyn. 17, 811-819
    • (2000) J. Biomol. Struct. Dyn. , vol.17 , pp. 811-819
    • Bansal, M.1    Kumar, S.2    Velavan, R.3
  • 38
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    • Strelkov, S. V., and Burkhard, P. (2002) Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation. J. Struct. Biol. 137, 54-64
    • (2002) J. Struct. Biol. , vol.137 , pp. 54-64
    • Strelkov, S.V.1    Burkhard, P.2
  • 40
    • 0027435278 scopus 로고
    • Diversity of intermediate filament structure. Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments
    • Steinert, P. M., Marekov, L. N., and Parry, D. A. (1993) Diversity of intermediate filament structure. Evidence that the alignment of coiled-coil molecules in vimentin is different from that in keratin intermediate filaments. J. Biol. Chem. 268, 24916-24925
    • (1993) J. Biol. Chem. , vol.268 , pp. 24916-24925
    • Steinert, P.M.1    Marekov, L.N.2    Parry, D.A.3
  • 41
    • 0027160195 scopus 로고
    • Keratin intermediate filament structure. Cross-linking studies yield quantitative information on molecular dimensions and mechanism of assembly
    • Steinert, P. M., Marekov, L. N., Fraser, R. D., and Parry, D. A. (1993) Keratin intermediate filament structure. Cross-linking studies yield quantitative information on molecular dimensions and mechanism of assembly. J. Mol. Biol. 230, 436-452
    • (1993) J. Mol. Biol. , vol.230 , pp. 436-452
    • Steinert, P.M.1    Marekov, L.N.2    Fraser, R.D.3    Parry, D.A.4
  • 42
    • 0030596170 scopus 로고    scopus 로고
    • Structure and assembly properties of the intermediate filament protein vimentin. The role of its head, rod, and tail domains
    • Herrmann, H., Häner, M., Brettel, M., Müller, S. A., Goldie, K. N., Fedtke, B., Lustig, A., Franke, W. W., and Aebi, U. (1996) Structure and assembly properties of the intermediate filament protein vimentin. The role of its head, rod, and tail domains. J. Mol. Biol. 264, 933-953
    • (1996) J. Mol. Biol. , vol.264 , pp. 933-953
    • Herrmann, H.1    Häner, M.2    Brettel, M.3    Müller, S.A.4    Goldie, K.N.5    Fedtke, B.6    Lustig, A.7    Franke, W.W.8    Aebi, U.9
  • 44
    • 0027476386 scopus 로고
    • The conserved H1 domain of the type II keratin 1 chain plays an essential role in the alignment of nearest neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two- To four-molecule level of structure
    • Steinert, P. M., and Parry, D. A. (1993) The conserved H1 domain of the type II keratin 1 chain plays an essential role in the alignment of nearest neighbor molecules in mouse and human keratin 1/keratin 10 intermediate filaments at the two- to four-molecule level of structure. J. Biol. Chem. 268, 2878-2887
    • (1993) J. Biol. Chem. , vol.268 , pp. 2878-2887
    • Steinert, P.M.1    Parry, D.A.2
  • 45
    • 18744388274 scopus 로고    scopus 로고
    • Sequence comparisons of intermediate filament chains. Evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1
    • Smith, T. A., Strelkov, S. V., Burkhard, P., Aebi, U., and Parry, D. A. (2002) Sequence comparisons of intermediate filament chains. Evidence of a unique functional/structural role for coiled-coil segment 1A and linker L1. J. Struct. Biol. 137, 128-145
    • (2002) J. Struct. Biol. , vol.137 , pp. 128-145
    • Smith, T.A.1    Strelkov, S.V.2    Burkhard, P.3    Aebi, U.4    Parry, D.A.5
  • 46
    • 0344096498 scopus 로고    scopus 로고
    • Characterization of distinct early assembly units of different intermediate filament proteins
    • Herrmann, H., Häner, M., Brettel, M., Ku, N. O., and Aebi, U. (1999) Characterization of distinct early assembly units of different intermediate filament proteins. J. Mol. Biol. 286, 1403-1420
    • (1999) J. Mol. Biol. , vol.286 , pp. 1403-1420
    • Herrmann, H.1    Häner, M.2    Brettel, M.3    Ku, N.O.4    Aebi, U.5


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