Localization of an Exchangeable GTP BZinding Site at the Plus End of Microtubules
- 20 August 1993
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 261 (5124) , 1044-1047
- https://doi.org/10.1126/science.8102497
Abstract
Microtubule polarity arises from the head-to-tail orientation of alpha-beta tubulin heterodimers in the microtubule lattice. The identity of the polypeptide at each end of the microtubule is unknown, but structural models predict that the beta-tubulin end contains an exchangeable guanosine triphosphate (GTP) binding site. When GTP-coated fluorescent beads were incubated with microtubules, they bound specifically to plus ends, suggesting that tubulin is oriented in microtubules with beta-tubulin toward the plus end.Keywords
This publication has 14 references indexed in Scilit:
- γ-Tubulin: the microtubule organizer?Trends in Cell Biology, 1992
- Microtubule Dynamics: Mechanism, Regulation, and FunctionAnnual Review of Cell Biology, 1991
- α‐, β‐, and γ‐tubulins: Sequence comparisons and structural constraintsCell Motility, 1991
- MOTOR PROTEINS OF CYTOPLASMIC MICROTUBULESAnnual Review of Biochemistry, 1990
- Asymmetric behavior of severed microtubule ends after ultraviolet-microbeam irradiation of individual microtubules in vitro.The Journal of cell biology, 1989
- Microtubule structure at 18 Å resolutionJournal of Molecular Biology, 1987
- Direct photoaffinity labeling of tubulin with guanosine 5'-triphosphateBiochemistry, 1985
- Unstained microtubules studied by cryo-electron microscopyJournal of Molecular Biology, 1985
- Polarity of microtubules nucleated by centrosomes and chromosomes of Chinese hamster ovary cells in vitroThe Journal of cell biology, 1980
- Microtubule Assembly and NucleationPublished by Elsevier ,1978