title: Examining F-actin interaction with intact talin and talin head and tail fragment using static and dynamic light scattering.
abstract: 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.
authors.affiliation: Department of Surgery, Surgery Research Laboratories, Massachusetts General Hospital, Harvard Medical School, Charlestown 02129, USA. goldman@helix.mgh.harvard.edu
authors.forename: W H
authors.initials: WH
authors.lastname: Goldmann
authors.forename: Z
authors.initials: Z
authors.lastname: Guttenberg
authors.forename: S
authors.initials: S
authors.lastname: Kaufmann
authors.forename: D
authors.initials: D
authors.lastname: Hess
authors.forename: R M
authors.initials: RM
authors.lastname: Ezzell
authors.forename: G
authors.initials: G
authors.lastname: Isenberg
mesh_terms: D000199:Actins / Q000737:chemistry*; D001665:Binding Sites; D006801:Humans; D008027:Light; D012542:Scattering, Radiation; D016608:Talin / Q000737:chemistry*
chemical_list: D000199:Actins; D016608:Talin