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Volumn 44, Issue 48, 2005, Pages 15898-15905

Conformational studies of the tetramerization site of human erythroid spectrin by cysteine-scanning spin-labeling EPR methods

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CONFORMATIONS; HYDROPHOBICITY; MOLECULAR DYNAMICS; PARAMAGNETIC RESONANCE; SCANNING;

EID: 28544443188     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051009m     Document Type: Article
Times cited : (12)

References (53)
  • 1
    • 17444415361 scopus 로고    scopus 로고
    • Spectrin, α-Actinin, and Dystrophin
    • Broderick, M. J., and Winder, S. J. (2005) Spectrin, α-Actinin, and Dystrophin, Adv. Protein Chem. 70, 203-46.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 203-246
    • Broderick, M.J.1    Winder, S.J.2
  • 2
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • Djinovic-Carugo, K., Gautel, M., Ylanne, J., and Young, P. (2002) The spectrin repeat: A structural platform for cytoskeletal protein assemblies, FEBS Lett. 513, 119-23.
    • (2002) FEBS Lett. , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylanne, J.3    Young, P.4
  • 3
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and Ankyrin-Based Pathways: Metazoan inventions for integrating cells into tissues
    • Bennett, V., and Baines, A. J. (2001) Spectrin and Ankyrin-Based Pathways: Metazoan inventions for integrating cells into tissues, Physiol. Rev. 81, 1353-92.
    • (2001) Physiol. Rev. , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 4
    • 0034974157 scopus 로고    scopus 로고
    • Spectrin oligomerization is cooperatively coupled to membrane assembly: A linkage targeted by many hereditary hemolytic anemias?
    • Giorgi, M., Cianci, C., Gallagher, P., and Morrow, J. S. (2001) Spectrin oligomerization is cooperatively coupled to membrane assembly: A linkage targeted by many hereditary hemolytic anemias? Exp. Mol. Pathol. 70, 215-30.
    • (2001) Exp. Mol. Pathol. , vol.70 , pp. 215-230
    • Giorgi, M.1    Cianci, C.2    Gallagher, P.3    Morrow, J.S.4
  • 5
    • 0034177578 scopus 로고    scopus 로고
    • The spectrin-based skeleton at the postsynaptic membrane of the neuromuscular junction
    • Kordeli, E. (2000) The spectrin-based skeleton at the postsynaptic membrane of the neuromuscular junction, Microsc. Res. Tech. 49, 101-7.
    • (2000) Microsc. Res. Tech. , vol.49 , pp. 101-107
    • Kordeli, E.1
  • 6
    • 0033953154 scopus 로고    scopus 로고
    • New insights into functions of erythroid proteins in nonerythroid cells
    • Gascard, P., and Mohandas, N. (2000) New insights into functions of erythroid proteins in nonerythroid cells, Curr. Opin. Hematol. 7, 123-9.
    • (2000) Curr. Opin. Hematol. , vol.7 , pp. 123-129
    • Gascard, P.1    Mohandas, N.2
  • 7
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers & mesh in the biosynthetic pathway
    • DeMatteis, M. A., and Morrow, J. S. (2000) Spectrin tethers & mesh in the biosynthetic pathway, J. Cell Sci. 113, 2331-43.
    • (2000) J. Cell Sci. , vol.113 , pp. 2331-2343
    • Dematteis, M.A.1    Morrow, J.S.2
  • 8
    • 0032704620 scopus 로고    scopus 로고
    • Discovery of nonerythroid spectrin to the demonstration of its key role in synaptic transmission
    • Goodman, S. R. (1999) Discovery of nonerythroid spectrin to the demonstration of its key role in synaptic transmission, Brain Res. Bull. 50, 345-6.
    • (1999) Brain Res. Bull. , vol.50 , pp. 345-346
    • Goodman, S.R.1
  • 9
    • 0032516894 scopus 로고    scopus 로고
    • A spectrin membrane skeleton of the Golgi complex
    • Beck, K. A., and Nelson, W. J. (1998) A spectrin membrane skeleton of the Golgi complex, Biochim. Biophys. Acta 1404, 153-60.
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 153-160
    • Beck, K.A.1    Nelson, W.J.2
  • 10
    • 0015863154 scopus 로고
    • Selective solubilization of proteins & phospholipids from red blood cell by non-ionic detergents
    • Yu, J., Fischman, D., and Steck, T. L. (1973) Selective solubilization of proteins & phospholipids from red blood cell by non-ionic detergents, J. Supramol. Struct. 1, 233-48.
    • (1973) J. Supramol. Struct. , vol.1 , pp. 233-248
    • Yu, J.1    Fischman, D.2    Steck, T.L.3
  • 11
    • 0020450486 scopus 로고
    • Spectrin domains: Proteolytic susceptibility as a probe of protein structure
    • Speicher, D. W., and Marchesi, V. T. (1982) Spectrin domains: Proteolytic susceptibility as a probe of protein structure, J. Cell. Biochem. 18, 479-92.
    • (1982) J. Cell. Biochem. , vol.18 , pp. 479-492
    • Speicher, D.W.1    Marchesi, V.T.2
  • 12
    • 0027478129 scopus 로고
    • Mutations involving the spectrin heterodimer contact site: Clinical expression & alterations in specific function
    • Delaunay, J., and Dhermy, D. (1993) Mutations involving the spectrin heterodimer contact site: Clinical expression & alterations in specific function, Semin. Hematol. 30, 21-33.
    • (1993) Semin. Hematol. , vol.30 , pp. 21-33
    • Delaunay, J.1    Dhermy, D.2
  • 14
    • 0019166431 scopus 로고
    • Identification of proteolytically resistant domains of human-erythroid spectrin
    • Speicher, D. W., Knowles, W. J., and Marchesi, V. T. (1980) Identification of proteolytically resistant domains of human-erythroid spectrin, Proc. Natl. Acad. Sci. U.S.A. 77, 5673-7.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 5673-5677
    • Speicher, D.W.1    Knowles, W.J.2    Marchesi, V.T.3
  • 15
    • 0027419729 scopus 로고
    • Location of the human red cell spectrin tetramer binding site & detection of a related "closed" hairpin loop dimer using proteolytic footprinting
    • Speicher, D. W., DeSilva, T. M., Speicher, K. D., Ursitti, J. A., Hembach, P., and Weglarz, L. (1993) Location of the human red cell spectrin tetramer binding site & detection of a related "closed" hairpin loop dimer using proteolytic footprinting, J. Biol. Chem. 268, 4227-35.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4227-4235
    • Speicher, D.W.1    Desilva, T.M.2    Speicher, K.D.3    Ursitti, J.A.4    Hembach, P.5    Weglarz, L.6
  • 16
    • 0019522402 scopus 로고
    • Self-assembly of spectrin oligomers in vitro: A basis for a dynamic cytoskeleton
    • Morrow, J., and Marchesi, V. T. (1981) Self-assembly of spectrin oligomers in vitro: A basis for a dynamic cytoskeleton, J. Cell Biol. 88, 463-8.
    • (1981) J. Cell Biol. , vol.88 , pp. 463-468
    • Morrow, J.1    Marchesi, V.T.2
  • 17
    • 0026470325 scopus 로고
    • Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides
    • DeSilva, T. M., Peng, K. C., Speicher, K. D., and Speicher, D. W. (1992) Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides, Biochemistry 31, 10872-8.
    • (1992) Biochemistry , vol.31 , pp. 10872-10878
    • Desilva, T.M.1    Peng, K.C.2    Speicher, K.D.3    Speicher, D.W.4
  • 18
    • 18944393929 scopus 로고    scopus 로고
    • Mutational Effects at the Tetramerization Site of Nonerythroid Alpha Spectrin
    • Sumandea, C. A., and Fung, L. W.-M. (2005) Mutational Effects at the Tetramerization Site of Nonerythroid Alpha Spectrin, Mol. Brain Res. 136, 81-90.
    • (2005) Mol. Brain Res. , vol.136 , pp. 81-90
    • Sumandea, C.A.1    Fung, L.W.-M.2
  • 19
    • 0035900013 scopus 로고    scopus 로고
    • αβ spectrin association: A model system to mimic helical bundling at the tetramerization site
    • Mehboob, S., Luo, B. H., and Fung, L. W.-M. (2001) αβ spectrin association: A model system to mimic helical bundling at the tetramerization site, Biochemistry 40, 12457-64.
    • (2001) Biochemistry , vol.40 , pp. 12457-12464
    • Mehboob, S.1    Luo, B.H.2    Fung, L.W.-M.3
  • 20
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher, D. W., and Marchesi, V. T. (1984) Erythrocyte spectrin is comprised of many homologous triple helical segments, Nature 311, 177-80.
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 21
    • 0038159470 scopus 로고    scopus 로고
    • Solution Structural Studies on Human Erythrocyte α Spectrin Tetramerization Site
    • Park, S., Caffrey, M., Johnson, M. E., and Fung, L. W.-M. (2003) Solution Structural Studies on Human Erythrocyte α Spectrin Tetramerization Site, J. Biol. Chem. 278, 21837-44.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21837-21844
    • Park, S.1    Caffrey, M.2    Johnson, M.E.3    Fung, L.W.-M.4
  • 23
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • Grum, V. L., Li, D., MacDonald, R. I., and Mondragon, A. (1999) Structures of two repeats of spectrin suggest models of flexibility, Cell 98, 523-35.
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 24
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell, W. L., Cafiso, D. S., and Altenbach, C. (2000) Identifying conformational changes with site-directed spin labeling, Nat. Struct. Biol. 7, 735-9.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 26
    • 0036251194 scopus 로고    scopus 로고
    • Residues at and before position 2072 (Thr) of β-spectrin are important for helical bundling of α-β spectrin complex
    • Luo, B. H., Mehboob, S., Hurtuk, M. G., Pipalia, N. H., and Fung, L. W.-M. (2002) Residues at and before position 2072 (Thr) of β-spectrin are important for helical bundling of α-β spectrin complex, Eur. J. Haematol. 68, 73-9.
    • (2002) Eur. J. Haematol. , vol.68 , pp. 73-79
    • Luo, B.H.1    Mehboob, S.2    Hurtuk, M.G.3    Pipalia, N.H.4    Fung, L.W.-M.5
  • 27
    • 0033978990 scopus 로고    scopus 로고
    • Spin-Label EPR Structural Studies of the N-terminus of α-Spectrin
    • Cherry, L., Menhart, N., and Fung, L. W.-M. (2000) Spin-Label EPR Structural Studies of the N-terminus of α-Spectrin, FEBS Lett. 466, 341-5.
    • (2000) FEBS Lett. , vol.466 , pp. 341-345
    • Cherry, L.1    Menhart, N.2    Fung, L.W.-M.3
  • 29
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaorab, H. S., Lietzow, M. A., Hideg, K., and Hubbell, W. L. (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics, Biochemistry 35, 7692-704.
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • Mchaorab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 30
    • 0004016501 scopus 로고
    • Comparison of Simple Potential Functions for Simulating Liquid Water
    • Jorgensen, W. L., Chandrasekhar, J., Madura, J., and Klein, M. L. (1983) Comparison of Simple Potential Functions for Simulating Liquid Water, J. Chem. Phys. 79, 926-35.
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.3    Klein, M.L.4
  • 32
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang, J., Cieplak, P., and Kollman, P. A. (2000) How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J. Comput. Chem. 21, 1049-74.
    • (2000) J. Comput. Chem. , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 33
    • 33846823909 scopus 로고
    • Particle mesh Ewaldan Nlog(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewaldan Nlog(N) method for Ewald sums in large systems, J. Chem. Phys. 98, 10089-92.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 34
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., Ciccotti, G., and Berendsen, H. J. C. (1977) Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes, J. Comput. Phys. 23, 327-41.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 36
    • 0033619698 scopus 로고    scopus 로고
    • Nitroxide scanning electron paramagnetic resonance of helices IV and V and the intervening loop in the lactose permease of Escherichia coli
    • Zhao, M., Zen, K. C., Hernandez-Borrell, J., Altenbach, C., Hubbell, W. L., and Kaback, H. R. (1999) Nitroxide scanning electron paramagnetic resonance of helices IV and V and the intervening loop in the lactose permease of Escherichia coli, Biochemistry 38, 15970-7.
    • (1999) Biochemistry , vol.38 , pp. 15970-15977
    • Zhao, M.1    Zen, K.C.2    Hernandez-Borrell, J.3    Altenbach, C.4    Hubbell, W.L.5    Kaback, H.R.6
  • 37
    • 0032444658 scopus 로고    scopus 로고
    • Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins
    • Buck, M. (1998) Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins, Q. Rev. Biophys. 31, 297-355.
    • (1998) Q. Rev. Biophys. , vol.31 , pp. 297-355
    • Buck, M.1
  • 38
    • 0035151189 scopus 로고    scopus 로고
    • Properties of 2,2,2-trifluoro-ethanol and water mixtures
    • Chitra, R., and Smith, P. E. (2001) Properties of 2,2,2-trifluoro-ethanol and water mixtures, J. Chem. Phys. 114, 426-35.
    • (2001) J. Chem. Phys. , vol.114 , pp. 426-435
    • Chitra, R.1    Smith, P.E.2
  • 39
    • 0034347797 scopus 로고    scopus 로고
    • Water-trifluorethanol mixtures: Some physicochemical properties
    • Gente, G., and La Mesa, C. (2000) Water-trifluorethanol mixtures: Some physicochemical properties, J. Surf. Chem. 29, 1159-72.
    • (2000) J. Surf. Chem. , vol.29 , pp. 1159-1172
    • Gente, G.1    La Mesa, C.2
  • 40
    • 0003877758 scopus 로고    scopus 로고
    • 84th ed., CRC Press, Cleveland, OH
    • Handbook of Chemistry & Physics (2003) 84th ed., pp 8-83, CRC Press, Cleveland, OH.
    • (2003) Handbook of Chemistry & Physics , pp. 8-83
  • 41
    • 0001248650 scopus 로고
    • α-helical coiled-coils: A widespread motif in proteins
    • Cohen, C., and Parry, D. A. D. (1986) α-helical coiled-coils: A widespread motif in proteins, Trends Biochem. Sci. 11, 245-8.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 245-248
    • Cohen, C.1    Parry, D.A.D.2
  • 43
  • 45
    • 0028240888 scopus 로고
    • Identification of three novel spectrin α I/74 mutations in hereditary elliptocytosis: Further support for a triple-stranded folding unit model of the spectrin heterodimer contact site
    • Parquet, N., Devaux, I., Boulanger, L., Galand, C., Boivin, P., Lecomte, M. C., Dhermy, D., and Garbarz, M. (1994) Identification of three novel spectrin α I/74 mutations in hereditary elliptocytosis: Further support for a triple-stranded folding unit model of the spectrin heterodimer contact site, Blood 84, 303-8.
    • (1994) Blood , vol.84 , pp. 303-308
    • Parquet, N.1    Devaux, I.2    Boulanger, L.3    Galand, C.4    Boivin, P.5    Lecomte, M.C.6    Dhermy, D.7    Garbarz, M.8
  • 46
    • 0025228664 scopus 로고
    • Hereditary pyropoikilocytosis and elliptocytosis in a white French family with the spectrin α I/74 variant related to a CGT to CAT codon change (Arg to His) at position 22 of the spectrin α I domain
    • Garbarz, M., Lecomte, M. C., Feo, C., Devaux, I., Picat, C., Lefebvre, C., Galibert, F., Gautero, H., Bournier, O., and Galand, C. (1990) Hereditary pyropoikilocytosis and elliptocytosis in a white French family with the spectrin α I/74 variant related to a CGT to CAT codon change (Arg to His) at position 22 of the spectrin α I domain, Blood 75, 1691-8.
    • (1990) Blood , vol.75 , pp. 1691-1698
    • Garbarz, M.1    Lecomte, M.C.2    Feo, C.3    Devaux, I.4    Picat, C.5    Lefebvre, C.6    Galibert, F.7    Gautero, H.8    Bournier, O.9    Galand, C.10
  • 47
    • 0030391717 scopus 로고    scopus 로고
    • Hematologically important mutations: Spectrin variants in hereditary elliptocytosis and hereditary pyropoikilocytosis
    • Gallagher, P., and Forget, B. G. (1996) Hematologically important mutations: Spectrin variants in hereditary elliptocytosis and hereditary pyropoikilocytosis, Blood Cells, Mol., Dis. 22, 254-8.
    • (1996) Blood Cells, Mol., Dis. , vol.22 , pp. 254-258
    • Gallagher, P.1    Forget, B.G.2
  • 48
    • 0025934799 scopus 로고
    • Four different mutations in codon 28 of α spectrin are associated with structurally and functionally abnormal spectrin α I/74 in hereditary elliptocytosis
    • Coetzer, T. L., Sahr, K., Prchal, J., Blacklock, H., Peterson, L., Koler, R., Doyle, J., Manaster, J., and Palek, J. (1991) Four different mutations in codon 28 of α spectrin are associated with structurally and functionally abnormal spectrin α I/74 in hereditary elliptocytosis, J. Clin. Invest. 88, 743-9.
    • (1991) J. Clin. Invest. , vol.88 , pp. 743-749
    • Coetzer, T.L.1    Sahr, K.2    Prchal, J.3    Blacklock, H.4    Peterson, L.5    Koler, R.6    Doyle, J.7    Manaster, J.8    Palek, J.9
  • 49
    • 0036660204 scopus 로고    scopus 로고
    • NMR Studies of Mutations at the Tetramerization Region of Human α Spectrin
    • Park, S., Johnson, M. E., and Fung, L. W.-M. (2002) NMR Studies of Mutations at the Tetramerization Region of Human α Spectrin, Blood 100, 283-8.
    • (2002) Blood , vol.100 , pp. 283-288
    • Park, S.1    Johnson, M.E.2    Fung, L.W.-M.3
  • 50
    • 0027438310 scopus 로고
    • Spectrin Cagliari: An Ala → Gly substitution in helix 1 of β spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer
    • Sahr, K. E., Coetzer, T. L., Moy, L. S., Derick, L. H., Chishti, A. H., Jarolim, P., Lorenzo, F., Miraglia del Giudice, E., Iolascon, A., and Gallanello, R. (1993) Spectrin Cagliari: An Ala → Gly substitution in helix 1 of β spectrin repeat 17 that severely disrupts the structure and self-association of the erythrocyte spectrin heterodimer, J. Biol. Chem. 268, 22656-62.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22656-22662
    • Sahr, K.E.1    Coetzer, T.L.2    Moy, L.S.3    Derick, L.H.4    Chishti, A.H.5    Jarolim, P.6    Lorenzo, F.7    Miraglia Del Giudice, E.8    Iolascon, A.9    Gallanello, R.10
  • 53
    • 0029848696 scopus 로고    scopus 로고
    • Stop codon in exon 30 (E2069X) of β-spectrin gene associated with hereditary elliptocytosis in spectrin Nagoya
    • Maillet, P., Inoue, T., Kanzaki, A., Yawata, A., Kato, K., Baklouti, F., Delaunay, J., and Yawata, Y. (1996) Stop codon in exon 30 (E2069X) of β-spectrin gene associated with hereditary elliptocytosis in spectrin Nagoya, Hum. Mutat. 8, 366-8.
    • (1996) Hum. Mutat. , vol.8 , pp. 366-368
    • Maillet, P.1    Inoue, T.2    Kanzaki, A.3    Yawata, A.4    Kato, K.5    Baklouti, F.6    Delaunay, J.7    Yawata, Y.8


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