摘要：SummaryThe effects of N-terminal acetylation of the high molecular weight tropomyosin isoforms Tpm1.6 and Tpm2.1 and the low molecular weight isoforms Tpm1.12, Tpm3.1, and Tpm4.2 on the actin affinity and the thermal stability of actin-tropomyosin cofilaments are described. Furthermore, we show how the exchange of cytoskeletal tropomyosin isoforms and their N-terminal acetylation affects the kinetic and chemomechanical properties of cytoskeletal actin-tropomyosin-myosin complexes. Our results reveal the extent to which the different actin-tropomyosin-myosin complexes differ in their kinetic and functional properties. The maximum sliding velocity of the actin filament as well as the optimal motor density for continuous unidirectional movement, parameters that were previously considered to be unique and invariant properties of each myosin isoform, are shown to be influenced by the exchange of the tropomyosin isoform and the N-terminal acetylation of tropomyosin.Graphical abstractDisplay OmittedHighlights•Tpm diversity is largely determined by sequences contributing to the overlap region•Global sequence differences are of greater importance than variable exon 6 usage•Tpm isoforms confer distinctly altered properties to cytoskeletal myosin motors•Cytoskeletal myosins are differentially affected by N-terminal acetylation of TpmBiological sciences; Biochemistry; Biomolecules; Protein; Biophysics
