[Interaction of bacterial flagella with myosin].
The interaction of isolated flagellar filaments of Bacillus brevis var. G.-B. P+ with skeletal muscle myosin has been investigated. Bacterial flagellar filaments co-precipitate with myosin at low ionic strength (at the conditions of myosin aggregation). Addition of bacterial flagellar filaments to myosin led to inhibition of its K+-EDTA- and Ca2+-ATPase activity, but had no influence on Mg2+-ATPase. Monomeric protein of bacterial flagella filaments (flagellin) did not co-precipitate with myosin and had no influence on its ATPase activity. The flagella filaments did not co-precipitate with myosin in the presence of F-actin if it was mixed with myosin before the filaments. If the flagella filaments were added to myosin solution before the addition of F-actin the amount of filaments and actin in myosin precipitate were comparable. In this case the presence of flagella filaments decreased activation of myosin Mg2+-ATPase by actin to 25-30%. Thus the bacterial flagellar filaments are able to interact with myosin and modify its ATPase activity. Probably, these properties of filaments are caused by resemblance of flagellin and actin. For instance, the unique origin of these proteins may be the reason of such resemblance.
D000251:Adenosine Triphosphatases / Q000032:analysis; D000818:Animals; D001407:Bacillus / Q000032:analysis / Q000502:physiology*; D001667:Binding, Competitive; D004591:Electrophoresis, Polyacrylamide Gel; D005407:Flagella / Q000032:analysis*; D005408:Flagellin / Q000032:analysis; D009068:Movement; D009132:Muscles / Q000032:analysis; D009218:Myosins / Q000032:analysis*; D011817:Rabbits
D005408:Flagellin; D000251:Adenosine Triphosphatases; D009218:Myosins
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