Identification of Ncd tail domain-binding sites on the tubulin dimer

Biochemical and Biophysical Research Communications

Volumn 305, Issue 3, 2003, Pages 523-528

  Karabay, A ^a,b   Walker, R A ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^b ISTANBUL TECHNICAL UNIVERSITY   (Turkey)

Author keywords

Kinesin; Microtubule; Ncd; Subtilisin; Tubulin

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN; DIMER; NON CLARET DISJUNCTIONAL PROTEIN; PROTEIN; SUBTILISIN; TUBULIN; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; HYPOTHESIS; MICROTUBULE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION;

EID: 0037902489     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00827-1     Document Type: Article

References (29)

1. Endow S.A., Henikoff S., Soler-Niedziela L. Mediation of meiotic and early mitotic chromosome segregation in Drosophila by a protein related to kinesin. Nature. 345:1990;81-83.
2. McDonald H.B., Goldstein L.S.B. Identification and characterization of a gene encoding a kinesin-like protein in Drosophila. Cell. 61:1990;991-1000.
3. Hatsumi M., Endow S.A. The Drosophila ncd microtubule motor protein is spindle-associated in meiotic and mitotic cells. J. Cell Sci. 103:1992;1013-1020.
4. Endow S.A. Chromosome distribution, molecular motors and the claret protein. Trends Genet. 9:1993;52-55.
5. Matthies H.J.G., McDonald H.B., Goldstein L.S.B., Theurkauf W.E. Anastral meiotic spindle morphogenesis: role of the non-claret disjunctional kinesin-like protein. J. Cell Biol. 134:1996;455-464.
6. Endow S.A., Komma D.J. Spindle dynamics during meiosis in Drosophila oocytes. J. Cell Biol. 137:1997;1321-1336.
7. Walker R.A., Salmon E.D., Endow S.A. The Drosophila claret segregation protein is a minus-end directed motor molecule. Nature. 347:1990;780-782.
8. McDonald H.B., Stewart R.J., Goldstein S.B. The kinesin-like ncd protein of Drosophila is a minus end-directed microtubule motor. Cell. 63:1990;1159-1165.
9. Karabay A., Walker R.A. Identification of microtubule binding sites in the Ncd tail domain. Biochemistry. 38:1999;1838-1849.
10. Goode B., Denis P.E., Panda D., Radeke M.J., Miller H.P., Wilson L., Feinstein S.C. Mol. Cell. Biol. 8:1997;353-365.
11. Karabay A., Walker R.A. The Ncd tail domain promotes microtubule assembly and stability. Biochem. Biophys. Res. Commun. 258:1999;39-43.
12. Chau M.-F., Radeke M.J., de Ines C., Barasoain I., Kohlstaedt L.A., Feinstein S.C. The microtubule-associated protein τ cross-links to two distinct sites on each α and β tubulin monomer via separate domains. Biochemistry. 37:1998;17692-17703.
13. Serrano L., Avila J., Maccioni R.B. Controlled proteolysis of tubulin by subtilisin: localization of the site for MAP2 interaction. Biochemistry. 23:1984;4675-4681.
14. Serrano L., Montejo de Garcini E., Hernandez M.A., Avila J. Localization of the tubulin binding site for τ protein. Eur. J. Biochem. 153:1985;595-600.
15. Marya P.K., Syed Z., Fraylich P.E., Eagles P.A. Kinesin and τ bind to distinct sites on microtubules. J. Cell Sci. 107:1994;339-344.
16. Melki R., Kerjan P., Waller J.P., Carlier M.F., Pantoloni D. Interaction of microtubule-associated proteins with microtubules: yeast lysyl- and valyl-tRNA synthetases and τ 218-235 synthetic peptide as model systems. Biochemistry. 30:1991;11536-11545.
17. Saoudi Y., Paintrand I., Multigner L., Job D. Stabilization and bundling of subtilisin-treated microtubules induced by microtubule associated proteins. J. Cell Sci. 108:1995;357-367.
18. Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100. kDa Anal. Biochem. 166:1987;368-379.
19. Theodorakis N.G., Cleveland D.W. Physical evidence for cotranslational regulation of β-tubulin mRNA degradation. Mol. Cell. Biol. 12:1992;791-799.
20. Lobert S., Correia J.J. Subtilisin cleavage of tubulin heterodimers and polymers. Arch. Biochem. Biophys. 296:1992;152-160.
21. Lobert S., Bettye S.H., Correia J. Multiple sites for subtilisin cleavage of tubulin: effects of divalent cations. Cell Motil. Cytoskeleton. 25:1993;282-297.
22. Redeker V., Melki R., Prome D., Le Caer J.P., Rossier J. Structure of tubulin C-terminal domain obtained by subtilisin treatment. The major α and β tubulin isotypes from pig brain are glutamylated. FEBS Lett. 313:1992;185-192.
23. Maccioni R.B., Serrano L., Avila J., Cann J.R. Characterization and structural aspects of the enhanced assembly of tubulin after removal of its carboxyl-terminal domain. Eur. J. Biochem. 156:1986;375-381.
24. De La Vina S., Andreu D., Medrano F.J., Nieto J.M., Andreu J.M. Tubulin structure probed with antibodies to synthetic peptides. Mapping of three major types of limited proteolysis fragments. Biochemistry. 27:1988;5352-5365.
25. Paschal B.M., Obar R.A., Vallee R.B. Interaction of brain cytoplasmic dynein and MAP2 with a common sequence at the C terminus of tubulin. Nature. 342:1989;569-572.
26. Gundersen G.G., Kalnoski M.H., Bulinski J.C. Distinct populations of microtubules: tyrosinated and nontyrosinated α tubulin are distributed differently in vivo. Cell. 38:1984;779-789.
27. Gimm M., Breitling F., Little M. Location of the epitope for the α-tubulin monoclonal antibody TU-O1. Biochim. Biophys. Acta. 914:1987;83-88.
28. Nogales E., Wolf S.G., Downing D.H. Structure of the. αβ tubulin dimer by electron crystallography Nature. 391:1998;199-203.
29. Nogales E., Whittaker M., Milligan R.A., Downing K.H. High-resolution model of the microtubule. Cell. 96:1999;79-88.