Examining F-actin interaction with intact talin and talin head and tail fragment using static and dynamic light scattering.
We examined the binding kinetics of intact talin and talin head and tail fragment with F-actin at pH 7.0 and at low ionic strength. We observed by a transient kinetic method a fast followed by a slower binding process for intact talin and talin tail fragment with filamentous actin. The latter can be attributed to F-actin cross-linking and/or bundling, which was observed in cosedimentation assays as well as by low shear viscometry and electron microscopy [Zhang, J., Robson, R. M., Schmidt, J. M. & Stromer, M. H. (1996) Biochem. Biophys. Res. Commun. 218, 530-537]. This finding is supported by dynamic light scattering measurements, indicating changes in internal actin filament dynamics due to cross-linking/bundling events with intact talin and talin tail fragment. No binding of the talin head fragment with F-actin was detected by either method.
Goldmann
W H
WH
Department of Surgery, Surgery Research Laboratories, Massachusetts General Hospital, Harvard Medical School, Charlestown 02129, USA. goldman@helix.mgh.harvard.edu
Guttenberg
Z
Z
Kaufmann
S
S
Hess
D
D
Ezzell
R M
RM
Isenberg
G
G
D000199:Actins / Q000737:chemistry*; D001665:Binding Sites; D006801:Humans; D008027:Light; D012542:Scattering, Radiation; D016608:Talin / Q000737:chemistry*
D000199:Actins; D016608:Talin