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Domain 2 of gelsolin binds directly to tropomyosin
Author(s) -
Maciver Sutherland K.,
Ternent Diane,
McLaughlin Paul J.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01507-6
Subject(s) - gelsolin , tropomyosin , actin , chemistry , protein filament , actin binding protein , microbiology and biotechnology , biophysics , biochemistry , biology , actin cytoskeleton , cytoskeleton , cell
Gelsolin is an actin filament severing protein composed of six similar structured domains that differ with respect to actin, calcium and polyphospho‐inositide binding. Previous work has established that gelsolin binds tropomyosin [Koepf, E.K. and Burtnick, L.D. (1992) FEBS Lett. 309, 56–58]. We have produced various specific gelsolin domains in Escherichia coli in order to establish which of the six domains binds tropomyosin. Gelsolin domains 1–3 (G1–3), G1–2 and G2 all bind tropomyosin in a pH and calcium insensitive manner whereas binding of G4–6 to tropomyosin was barely detectable under the conditions tested. We conclude that gelsolin binds tropomyosin via domain 2 (G2).