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J. Biol. Chem., Vol. 263, Issue 2, 722-727, Jan, 1988
E Andre, F Lottspeich, M Schleicher and A Noegel
cDNA clones encoding the actin filament severing protein severin from
Dictyostelium discoideum were isolated from a cDNA library in lambda gt 11
using monoclonal antibodies. Comparison of the deduced amino acid sequence
with the sequence of a severin peptide indicated that the complete coding
region of severin is contained in the isolated clones. Severin, a 39.9-kDa
protein, is encoded by one gene in D. discoideum. An mRNA of approximately
1.4 kilobases is present throughout the developmental cycle of D.
discoideum. The amino acid sequence of severin contains a region highly
homologous to a conserved sequence in villin and gelsolin, two proteins of
similar function isolated from vertebrates. This homologous region is
believed to participate in the actin filament severing activity of these
proteins. Comparison of the severin sequence to the entire gelsolin
sequence shows remarkable homologies pointing to a common origin from an
ancestral gene from which gelsolin has been derived by a duplication.
Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains
Max-Planck-Institut fur Biochemie, Martinsried, Federal Republic of Germany.
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