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Robaszkiewicz, Katarzyna, 2023, "Troponin and myopathy-linked mutation in TPM3 inhibit depolymerization of thin filament caused by cofilin-2", https://doi.org/10.18150/ZDLMTM, RepOD, V1
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The files are a collection of raw experimental data that were used to prepare figures which are to be published in the article under the title: "Troponin and myopathy-linked mutation in TPM3 inhibit depolymerization of thin filament caused by cofilin-2" by Katarzyna Robaszkiewicz, Julia Wróbel and Joanna Moraczewska in . Int. J. Mol. Sci. 2023, 24. Analyses were performed using thin filaments reconstituted from muscle actin, Tn, and recombinant wild -type or mutant Tpm3.12 variants. Data were obtained with the used of co-sedimentation assays and fluorescence microscopy observation of actin filaments depolymerization induced by cofilin-2. Actin-cofilin-2 binding affinity was obtained by measuring the amount of cofilin-2 that cosediments with actin filaments covered by Tpm variants alone or by Tpm-Tn complex in the absence or presence of Ca2+. Cofilin-induced dissociation of Tpm from the filament was obtained from the SDS gels used to separate proteins collected in pellets at increasing cofilin-2 concentrations. Severing and depolymerization rates of actin filaments with tetramethylrhodamine cadaverine (TRC) by cofilin-2 were observed directly using an Olympus IX83 inverted fluorescence microscope (magnification 100×).
thin filament, tropomyosin, myopathy, troponin, cofilin-2, actin
CC0 Creative Commons Zero 1.0
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