Binding of dynein 21 S ATPase to microtubules. Effects of ionic conditions and substrate analogs.
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Binding of 21 S dynein ATPase isolated from Tetrahymena cilia to B subfibers of microtubule doublets was used as a model system to study dynein-tubulin interactions and their relationship to the microtubule-based sliding filament mechanism. Binding of 21 S dynein to both A and B microtubule subfibers is supported by monovalent as well as divalent ions. Monovalent cation chlorides support dynein binding to B subfibers with the specificity Li greater than Na congruent to K congruent to Rb congruent to Cs congruent to choline. The corresponding sodium or potassium halides follow the order F greater than Cl greater than Br greater than I. However, an optimal binding concentration of 40 mM KCl supports only 55% of the protein binding which takes place in 3 mM MgSO4 and does not stabilize dynein cross-bridges when whole axonemes are fixed for electron microscopy. Divalent metal ion chlorides (MgCl2, CaCl2, SrCl2, and BaCl2) have nearly equivalent effects at a concentration of 6 mM; all support about 140% of the binding observed in 6 mM MgSO4. The binding data suggest negative cooperativity or the presence of more than one class of dynein binding sites on the microtubule lattice. Low concentrations of MgATP2- induce dissociation of dynein bound to B subfibers in either 6 mM MgSO4 or 40 mM KCl. ADP, Pi, PPi, and AMP-PCH2P are unable to induce dynein dissociation, while AMP-PNHP and ATP4- both cause dynein release from B subfiber sites. The half-maximal sensitivities of the tubulin-dy…
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NEM inhibits force generation by dynein, as well as dynein's ability to bind to microtubules.
“While NEM inhibits force generation by dynein (Mitchell and Warner, 1981; Cosson and Gibbons, 1978), as well as dynein’s ability to bind to microtubules (Shimizu and Kimura, 1974)”
From Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility (1985) · cites this paper as Mitchell and Warner, 1981
AMP-PNP decreases the affinity of dynein for microtubules and of myosin for actin.
“While AMP-PNP decreases the affinity of dynein for microtubules (Mitchell and Warner, 1981) and of myosin for actin (Greene and Eisenberg, 1980)”
From Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility (1985) · cites this paper as Mitchell and Warner, 1981
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- Authors
- Mitchell, D. R., & Warner, F. D.
- Affiliations
- Yale University (US)
- ORCID
- Mitchell, D.R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1981-12
- Volume
- 256
- Issue
- 23
- Pages
- 12535-12544
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1533843471
- Cited by
- 42
- References
- 41
- FWCI
- 1.53
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- doublet microtubules, ionic environment, divalent cations, monovalent cations, ATP binding, AMP-PNP, sliding filament mechanism, axoneme, N-ethylmaleimide
- MeSH terms
- Adenosine Triphosphatases, Animals, Cations, Divalent, Cations, Monovalent, Cilia, Dyneins, Kinetics, Microscopy, Electron, Microtubules, Molecular Weight, Protein Binding, Tetrahymena, Tubulin
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