메뉴 건너뛰기




Volumn 1383, Issue 1, 1998, Pages 111-122

Probing the ATP binding site of tubulin with thiotriphosphate analogues of ATP

Author keywords

ATP S; dATP S; Microtubule; Tubulin

Indexed keywords

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; DEOXYADENOSINE TRIPHOSPHATE; DEOXYGUANOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE DERIVATIVE; TUBULIN;

EID: 0032478047     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(97)00193-3     Document Type: Article
Times cited : (3)

References (43)
  • 1
    • 0030222340 scopus 로고    scopus 로고
    • Getting to the heart of β-tubulin
    • Burns R.C., Farrell K.W. Getting to the heart of β-tubulin. Trends Cell Biol. 6:1996;297-303.
    • (1996) Trends Cell Biol. , vol.6 , pp. 297-303
    • Burns, R.C.1    Farrell, K.W.2
  • 3
    • 0002445059 scopus 로고
    • Microtubule dynamics in vitro
    • in: J.S. Hyans, C.W. Lloyd (Eds.) Liss, New York
    • P.M. Bayley, K.K. Sharma, S.R. Martin, Microtubule dynamics in vitro, in: J.S. Hyans, C.W. Lloyd (Eds.), Microtubules, Liss, New York, 1993, pp. 111-137.
    • (1993) Microtubules , pp. 111-137
    • Bayley, P.M.1    Sharma, K.K.2    Martin, S.R.3
  • 6
    • 0019436432 scopus 로고
    • Kinetic analysis of guanosine 5′-triphosphate hydrolysis associated with tubulin polymerization
    • Carlier M.F., Pantaloni D. Kinetic analysis of guanosine 5′-triphosphate hydrolysis associated with tubulin polymerization. Biochemistry. 20:1981;1918-1924.
    • (1981) Biochemistry , vol.20 , pp. 1918-1924
    • Carlier, M.F.1    Pantaloni, D.2
  • 7
    • 0028241739 scopus 로고
    • Microtubule dynamics modulated by guanosine triphosphate hydrolysis activity of β-tubulin
    • Davis A., Sage C.R., Dougherty C.A., Farrell K.W. Microtubule dynamics modulated by guanosine triphosphate hydrolysis activity of β-tubulin. Science. 264:1994;839-842.
    • (1994) Science , vol.264 , pp. 839-842
    • Davis, A.1    Sage, C.R.2    Dougherty, C.A.3    Farrell, K.W.4
  • 8
    • 0027944049 scopus 로고
    • Interaction of tubulin with guanosine 5′-O-(1-triotriphosphate) diastereoisomers: Specificity of the α-phosphate binding region
    • Xu S., Gaskin F. Interaction of tubulin with guanosine 5′-O-(1-triotriphosphate) diastereoisomers: Specificity of the α-phosphate binding region. Biochemistry. 33:1994;11884-11890.
    • (1994) Biochemistry , vol.33 , pp. 11884-11890
    • Xu, S.1    Gaskin, F.2
  • 9
    • 0023802267 scopus 로고
    • Stereoselectivity of the guanyl-exchangeable nucleotide-binding site of tubulin probed by guanosine 5′-O-(2-thiotriphosphate) diastereoisomers
    • Roychowdhury S., Gaskin F. Stereoselectivity of the guanyl-exchangeable nucleotide-binding site of tubulin probed by guanosine 5′-O-(2-thiotriphosphate) diastereoisomers. Biochemistry. 27:1988;7799-7805.
    • (1988) Biochemistry , vol.27 , pp. 7799-7805
    • Roychowdhury, S.1    Gaskin, F.2
  • 10
    • 0019852251 scopus 로고
    • Assembly of tubulin with nucleotide analogues
    • Kirsch M., Yarbrough L.R. Assembly of tubulin with nucleotide analogues. J. Biol. Chem. 256:1981;106-111.
    • (1981) J. Biol. Chem. , vol.256 , pp. 106-111
    • Kirsch, M.1    Yarbrough, L.R.2
  • 11
    • 0021198812 scopus 로고
    • Guanosine 5′-O-(3-thiotriphosphate), a potent nucleotide inhibitor of microtubule assembly
    • Hamel E., Lin C.M. Guanosine 5′-O-(3-thiotriphosphate), a potent nucleotide inhibitor of microtubule assembly. J. Biol. Chem. 259:1984;11060-11069.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11060-11069
    • Hamel, E.1    Lin, C.M.2
  • 12
    • 0022886679 scopus 로고
    • Magnesium requirements for guanosine 5′-O-(3-thiotriphosphate) induced assembly of microtubule protein and tubulin
    • Roychowdhury S., Gaskin F. Magnesium requirements for guanosine 5′-O-(3-thiotriphosphate) induced assembly of microtubule protein and tubulin. Biochemistry. 25:1986;7847-7853.
    • (1986) Biochemistry , vol.25 , pp. 7847-7853
    • Roychowdhury, S.1    Gaskin, F.2
  • 13
    • 0021891882 scopus 로고
    • Nucleoside phosphorothioates
    • Eckstein F. Nucleoside phosphorothioates. Ann. Rev. Biochem. 54:1985;367-402.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 367-402
    • Eckstein, F.1
  • 14
    • 0021923785 scopus 로고
    • Structures of manganese(II) complexes with ATP, ADP, and phosphocreatine in the reactive central complexes with creatine kinase: Electron paramagnetic resonance studies with oxygen-17-labeled ligands
    • Leyh T.S., Goodhart P.J., Nguyen A.C., Kenyon G.L., Reed G.H. Structures of manganese(II) complexes with ATP, ADP, and phosphocreatine in the reactive central complexes with creatine kinase: Electron paramagnetic resonance studies with oxygen-17-labeled ligands. Biochemistry. 24:1985;308-316.
    • (1985) Biochemistry , vol.24 , pp. 308-316
    • Leyh, T.S.1    Goodhart, P.J.2    Nguyen, A.C.3    Kenyon, G.L.4    Reed, G.H.5
  • 15
    • 0021769550 scopus 로고
    • 2+ complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of MgATP and MgADP
    • 2+ complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of MgATP and MgADP. Biochemistry. 23:1984;5262-5271.
    • (1984) Biochemistry , vol.23 , pp. 5262-5271
    • Pecoraro, V.L.1    Hermes, J.D.2    Cleland, W.W.3
  • 16
    • 0022418143 scopus 로고
    • Bond order and charge localization in nucleoside phosphorothioates
    • Frey P.A., Sammons R.D. Bond order and charge localization in nucleoside phosphorothioates. Science. 228:1985;541-545.
    • (1985) Science , vol.228 , pp. 541-545
    • Frey, P.A.1    Sammons, R.D.2
  • 17
    • 0022478487 scopus 로고
    • Tubulin polymerization with ATP is mediated through the exchangeable GTP site
    • Duanmu C., Lin C.M., Hamel E. Tubulin polymerization with ATP is mediated through the exchangeable GTP site. Biochim. Biophys. Acta. 881:1986;113-123.
    • (1986) Biochim. Biophys. Acta , vol.881 , pp. 113-123
    • Duanmu, C.1    Lin, C.M.2    Hamel, E.3
  • 18
    • 0024533465 scopus 로고
    • Assembly of pure tubulin in the absence of free GTP: Effect of magnesium, glycerol, ATP, and the nonhydrolyzable GTP analogues
    • O'Brien E.T., Erickson H.P. Assembly of pure tubulin in the absence of free GTP: Effect of magnesium, glycerol, ATP, and the nonhydrolyzable GTP analogues. Biochemistry. 28:1989;1413-1422.
    • (1989) Biochemistry , vol.28 , pp. 1413-1422
    • O'Brien, E.T.1    Erickson, H.P.2
  • 19
    • 0025305348 scopus 로고
    • Re-examination of the role of nonhydrolyzable guanosine 5′-triphosphate analogues in tubulin polymerization: Reaction conditions are a critical factor for effective interactions at the exchangeable nucleotide site
    • Hamel E., Lin C.M. Re-examination of the role of nonhydrolyzable guanosine 5′-triphosphate analogues in tubulin polymerization: Reaction conditions are a critical factor for effective interactions at the exchangeable nucleotide site. Biochemistry. 29:1990;2720-2729.
    • (1990) Biochemistry , vol.29 , pp. 2720-2729
    • Hamel, E.1    Lin, C.M.2
  • 20
    • 0025060807 scopus 로고
    • GTP analogues interact with the tubulin exchangeable site during assembly and upon binding
    • Mejillano M.R., Barton J.S., Nath J.P., Himes R.H. GTP analogues interact with the tubulin exchangeable site during assembly and upon binding. Biochemistry. 29:1990;1208-1216.
    • (1990) Biochemistry , vol.29 , pp. 1208-1216
    • Mejillano, M.R.1    Barton, J.S.2    Nath, J.P.3    Himes, R.H.4
  • 21
    • 0027495732 scopus 로고
    • Interaction of ant-ATP with tubulin: Evidence for ATP competition for the GTP E-site on tubulin
    • Rai S.S., Kasturi S.R. Interaction of ant-ATP with tubulin: Evidence for ATP competition for the GTP E-site on tubulin. Arch. Biochem. Biophys. 306:1993;133-138.
    • (1993) Arch. Biochem. Biophys. , vol.306 , pp. 133-138
    • Rai, S.S.1    Kasturi, S.R.2
  • 22
    • 0030067616 scopus 로고    scopus 로고
    • Nucleotide binding to tubulin-investigations by nuclear magnetic resonance spectroscopy
    • Rai S.S., Kuchoo K., Kasturi S.R. Nucleotide binding to tubulin-investigations by nuclear magnetic resonance spectroscopy. Biochim. Biophys. Acta. 1292:1996;77-88.
    • (1996) Biochim. Biophys. Acta , vol.1292 , pp. 77-88
    • Rai, S.S.1    Kuchoo, K.2    Kasturi, S.R.3
  • 23
    • 0019986789 scopus 로고
    • Effect of ATP on the kinetics of microtubule assembly
    • Zabrecky J.R., Cole R.D. Effect of ATP on the kinetics of microtubule assembly. J. Biol. Chem. 257:1982;4633-4638.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4633-4638
    • Zabrecky, J.R.1    Cole, R.D.2
  • 24
    • 0028124183 scopus 로고
    • Identification of peptides within the base binding domains of the GTP- and ATP-specific binding sites of tubulin
    • Jayaram B., Haley B.E. Identification of peptides within the base binding domains of the GTP- and ATP-specific binding sites of tubulin. J. Biol. Chem. 269:1994;3233-3242.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3233-3242
    • Jayaram, B.1    Haley, B.E.2
  • 26
    • 0022475610 scopus 로고
    • Separation of assembly-competent tubulin from brain microtubule protein preparation using a fast performance liquid chromatography procedure
    • Roychowdhury S., Gaskin F. Separation of assembly-competent tubulin from brain microtubule protein preparation using a fast performance liquid chromatography procedure. J. Neurochem. 46:1986;1399-1405.
    • (1986) J. Neurochem. , vol.46 , pp. 1399-1405
    • Roychowdhury, S.1    Gaskin, F.2
  • 28
    • 0016344556 scopus 로고
    • Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules
    • Gaskin F., Cantor C.R., Shelanski M.L. Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules. J. Mol. Biol. 89:1974;737-755.
    • (1974) J. Mol. Biol. , vol.89 , pp. 737-755
    • Gaskin, F.1    Cantor, C.R.2    Shelanski, M.L.3
  • 29
    • 0017287188 scopus 로고
    • Synthesis and properties of diastereoisomers of adenosine 5′-(O-1-thiotriphosphate) and adenosine 5′-(O-2-thiotriphosphate)
    • Eckstein F., Good R. Synthesis and properties of diastereoisomers of adenosine 5′-(O-1-thiotriphosphate) and adenosine 5′-(O-2-thiotriphosphate). Biochemistry. 15:1976;1685-1691.
    • (1976) Biochemistry , vol.15 , pp. 1685-1691
    • Eckstein, F.1    Good, R.2
  • 30
    • 0018114030 scopus 로고
    • Chromium(III)-nucleotide complexes as probes of the guanosine 5′-triphosphate-induced microtubule assembly
    • MacNeal R.K., Purich D.L. Chromium(III)-nucleotide complexes as probes of the guanosine 5′-triphosphate-induced microtubule assembly. Arch. Biochem. Biophys. 191:1978;233-243.
    • (1978) Arch. Biochem. Biophys. , vol.191 , pp. 233-243
    • MacNeal, R.K.1    Purich, D.L.2
  • 31
    • 0027248960 scopus 로고
    • Purification and biochemical characterization of tubulin from the budding yeast Saccharomyces cerevisiae
    • Davis A., Sage C.R., Wilson L., Farrell K.W. Purification and biochemical characterization of tubulin from the budding yeast Saccharomyces cerevisiae. Biochemistry. 32:1993;8823-8835.
    • (1993) Biochemistry , vol.32 , pp. 8823-8835
    • Davis, A.1    Sage, C.R.2    Wilson, L.3    Farrell, K.W.4
  • 32
    • 0343488814 scopus 로고    scopus 로고
    • Tubulin assembly in the presence of calcium ions and taxol: Microtubule bundling and formation of macrotubule-ring complexes
    • Vater W., Bohm K.J., Unger E. Tubulin assembly in the presence of calcium ions and taxol: Microtubule bundling and formation of macrotubule-ring complexes. Cell Motil. Cytoskeleton. 36:1997;76-83.
    • (1997) Cell Motil. Cytoskeleton , vol.36 , pp. 76-83
    • Vater, W.1    Bohm, K.J.2    Unger, E.3
  • 33
    • 0017407054 scopus 로고
    • Tubulin sulfhydryl groups and polymerization in vitro
    • Wallin M., Larsson H., Edstrom A. Tubulin sulfhydryl groups and polymerization in vitro. Exp. Cell Res. 107:1977;219-225.
    • (1977) Exp. Cell Res. , vol.107 , pp. 219-225
    • Wallin, M.1    Larsson, H.2    Edstrom, A.3
  • 34
    • 0017663070 scopus 로고
    • Zinc ion-induced assembly of tubulin
    • Gaskin F., Kress Y. Zinc ion-induced assembly of tubulin. J. Biol. Chem. 19:1977;6918-6924.
    • (1977) J. Biol. Chem. , vol.19 , pp. 6918-6924
    • Gaskin, F.1    Kress, Y.2
  • 35
    • 0019516870 scopus 로고
    • In vitro microtubule assembly regulation by divalent cations and nucleotides
    • Gaskin F. In vitro microtubule assembly regulation by divalent cations and nucleotides. Biochemistry. 20:1981;1318-1322.
    • (1981) Biochemistry , vol.20 , pp. 1318-1322
    • Gaskin, F.1
  • 37
    • 0017253965 scopus 로고
    • Microtubular protein reaction with nucleotides
    • Jacobs M., Caplow M. Microtubular protein reaction with nucleotides. Biochem. Biophys. Res. Comm. 68:1976;127-135.
    • (1976) Biochem. Biophys. Res. Comm. , vol.68 , pp. 127-135
    • Jacobs, M.1    Caplow, M.2
  • 38
    • 0018695962 scopus 로고
    • Determination of free and bound microtubular protein and guanine nucleotide under equilibrium conditions
    • Zeeberg B., Caplow M. Determination of free and bound microtubular protein and guanine nucleotide under equilibrium conditions. Biochemistry. 18:1979;3880-3886.
    • (1979) Biochemistry , vol.18 , pp. 3880-3886
    • Zeeberg, B.1    Caplow, M.2
  • 39
    • 0020081719 scopus 로고
    • Binding of ATP to tubulin
    • Zabrecky J.R., Cole R.D. Binding of ATP to tubulin. Nature. 296:1982;757-758.
    • (1982) Nature , vol.296 , pp. 757-758
    • Zabrecky, J.R.1    Cole, R.D.2
  • 40
    • 0028930562 scopus 로고
    • In vitro assembly of microtubule protein with GTP and 2′dGTP: Kinetic evidence for a preassembly conformational change
    • Burns R.G., Symmons M.F. In vitro assembly of microtubule protein with GTP and 2′dGTP: Kinetic evidence for a preassembly conformational change. Biochemistry. 34:1995;2302-2308.
    • (1995) Biochemistry , vol.34 , pp. 2302-2308
    • Burns, R.G.1    Symmons, M.F.2
  • 42
    • 0029975170 scopus 로고    scopus 로고
    • Calcium and gadolinium ions stimulate the GTPase activity of purified chicken brain tubulin through a conformational change
    • Soto C., Rodriguez P.H., Monasterio O. Calcium and gadolinium ions stimulate the GTPase activity of purified chicken brain tubulin through a conformational change. Biochemistry. 35:1996;6337-6344.
    • (1996) Biochemistry , vol.35 , pp. 6337-6344
    • Soto, C.1    Rodriguez, P.H.2    Monasterio, O.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.