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Fig. 5. In vitro interactions of plectin 1 and β-synemin with F-actin. Bindings of plectin CHD
and β-synemin Tail N1 fragments to F-actin were demonstrated by actin co-sedimentation assay. After centrifugation, most of CHD fragments (3 µM) were found in the pellet (P) in the presence of F-actin (6 µM), whereas they remained in the supernatant (S) in the absence of actin (lanes 2 and 3). Small amounts of β-synemin Tail N1 fragments were sedimented in the presence of F-actin (15 µM and 30 µM β-synemin in lanes 4 and 5, respectively), while in the absence of F-actin, the Tail N1 fragments (30 µM) were observed mostly in the supernatant (lanes 6). Even in the presence of a 10-fold molar excess of Tail N1 fragments (30 µM), CHD fragments were still found mostly in the pellet together with F-actin (compare lanes 7 with lanes 8).
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