Biomaterial Database

Activation of dynein 1 adenosine triphosphatase by monovalent salts and inhibition by vanadate. 1986

J A Evans, and G Mocz, and I R Gibbons

The ATPase activity of native dynein 1 from sea urchin sperm flagella is activated reversibly by inorganic monovalent chlorides with the magnitude of activation being nearly independent of the cation below 0.3 M. At higher concentrations, activation increases in the order LiCl greater than NH4Cl greater than NaCl greater than KCl, with the maximum occurring at about 0.8 M in all cases. The sodium halides activate reversibly in the order NaI greater than NaBr greater than NaCl, but NaF is strongly inhibitory. The presence of the organic anions formate, acetate, or propionate favors the native low ATPase activity state, with lithium acetate giving little activation at up to 1 M and sodium acetate partially reversing the activation due to simultaneous presence of 0.6 M NaCl. The sedimentation rate of the dynein does not change between 0.2 and 0.8 M NaCl or sodium acetate, suggesting that the effects of the anions on ATPase activity are due to local changes near the catalytic site, rather than to large-scale changes in the molecular structure. All the agents that activate the dynein ATPase, either reversibly (halides) or irreversibly (Triton X-100), decrease its sensitivity to inhibition by vanadate, consistent with ATPase activation being the result of a decreased stability of the dynein. ADP.Pi kinetic intermediate that is thought to bind vanadate at the gamma-Pi site and act as a dead-end kinetic block. Although many divalent cations, including Mg2+, Mn2+, Fe2+, Co2+, Ni2+, Zn2+, Ca2+, and Sr2+, can support dynein ATPase activity, the magnitude of ATPase increase observed upon treatment with Triton X-100 is greatest with Mg2+ and Mn2+, which are also the only cations capable of supporting the motility of demembranated flagella at rates similar to those observed in vivo.

UI	MeSH Term	Description	Entries
D008297	Male		Males
D002412	Cations	Positively charged atoms, radicals or groups of atoms which travel to the cathode or negative pole during electrolysis.	Cation
D004398	Dyneins	A family of multi-subunit cytoskeletal motor proteins that use the energy of ATP hydrolysis, generated by a ring of AAA ATPASES in the dynein heavy chain, to power a variety of cellular functions. Dyneins fall into two major classes based upon structural and functional criteria.	ATPase, Dynein,Adenosinetriphosphatase, Dynein,Dynein,Dynein ATPase,Dynein Adenosinetriphosphatase,Dynein Heavy Chain,Dynein Intermediate Chain,Dynein Light Chain,Dynein Light Intermediate Chain,Adenosine Triphosphatase, Dynein,Dynein Heavy Chains,Dynein Intermediate Chains,Dynein Light Chains,Dynein Light Intermediate Chains,Chain, Dynein Heavy,Chain, Dynein Intermediate,Chain, Dynein Light,Chains, Dynein Heavy,Chains, Dynein Intermediate,Chains, Dynein Light,Dynein Adenosine Triphosphatase,Heavy Chain, Dynein,Heavy Chains, Dynein,Intermediate Chain, Dynein,Intermediate Chains, Dynein,Light Chain, Dynein,Light Chains, Dynein
D004789	Enzyme Activation	Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.	Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D000251	Adenosine Triphosphatases	A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.	ATPases,Adenosinetriphosphatase,ATPase,ATPase, DNA-Dependent,Adenosine Triphosphatase,DNA-Dependent ATPase,DNA-Dependent Adenosinetriphosphatases,ATPase, DNA Dependent,Adenosinetriphosphatases, DNA-Dependent,DNA Dependent ATPase,DNA Dependent Adenosinetriphosphatases,Triphosphatase, Adenosine
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D000838	Anions	Negatively charged atoms, radicals or groups of atoms which travel to the anode or positive pole during electrolysis.	Anion
D012617	Sea Urchins	Somewhat flattened, globular echinoderms, having thin, brittle shells of calcareous plates. They are useful models for studying FERTILIZATION and EMBRYO DEVELOPMENT.	Echinoidea,Sand-Dollar,Clypeasteroida,Sand Dollars,Clypeasteroidas,Dollar, Sand,Dollars, Sand,Echinoideas,Sand Dollar,Sand-Dollars,Sea Urchin,Urchin, Sea,Urchins, Sea
D014638	Vanadates	Oxyvanadium ions in various states of oxidation. They act primarily as ion transport inhibitors due to their inhibition of Na(+)-, K(+)-, and Ca(+)-ATPase transport systems. They also have insulin-like action, positive inotropic action on cardiac ventricular muscle, and other metabolic effects.	Decavanadate,Metavanadate,Orthovanadate,Oxyvanadium,Vanadyl,Monovanadate,Sodium Vanadate,Vanadate,Vanadate, Sodium
D014639	Vanadium	A metallic element with the atomic symbol V, atomic number 23, and atomic weight 50.94. It is used in the manufacture of vanadium steel. Prolonged exposure can lead to chronic intoxication caused by absorption usually via the lungs.	Vanadium-51,Vanadium 51