Common and distinct tubulin binding sites for microtubule-associated proteins
| Autor: | Uriel Z. Littauer, Herwig Ponstingl, David Giveon, Irith Ginzburg, Marion Thierauf |
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| Rok vydání: | 1986 |
| Předmět: |
Binding Sites
Multidisciplinary Swine Microtubule-associated protein Ligand binding assay macromolecular substances Plasma protein binding Biology Peptide Fragments Rats Tubulin binding Molecular Weight Tubulin Polyglycylation Biochemistry Microtubule biology.protein Animals Binding site Microtubule-Associated Proteins Oligopeptides Research Article Protein Binding |
| Zdroj: | Proceedings of the National Academy of Sciences. 83:7162-7166 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.83.19.7162 |
| Popis: | A specific binding assay was developed that monitors the interaction of 125I-labeled microtubule-associated proteins (MAPs) with tubulin or its fragments bound to nitrocellulose membrane. To identify the tubulin-binding domains for MAPs we have examined the binding of rat brain 125I-labeled MAP2 or 125I-labeled tau factors to 60 peptides derived from porcine alpha- and beta-tubulin. MAP2 and tau factors specifically interacted with two peptides derived from the carboxyl-terminal region of beta-tubulin, which are located between positions 392-445 and 416-445. In addition, there is a distinct tau-binding site at the amino-terminal region of alpha-tubulin. tau factors but not MAP2 displayed strong interaction with a peptide derived from the amino-terminal domain of alpha-tubulin between positions 1 and 75. To narrow down the location of the beta-tubulin binding site that is common to MAP2 and tau factors, we have synthesized five peptides that are homologous to the corresponding sequence from the porcine or rat carboxyl-terminal region. Binding studies with the synthetic peptides suggest that amino acid residues 434-440 of beta-tubulin are crucial for the interaction of MAP2 and tau factors. |
| Databáze: | OpenAIRE |
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