The complete sequence of a 40-kDa actin-modulating protein from the earthworm Lumbricus terrestris.
The complete primary structure of a 40-kDa actin-modulating protein from the earthworm Lumbricus terrestris is presented. A muscle-specific cDNA library of the earthworm was constructed and screened with a specific DNA probe obtained by polymerase chain reaction considering information from peptide sequencing. A full-length clone with a coding region of 1098 bp was isolated. The deduced polypeptide sequence of 366 amino acids (41457 Da) reveals the segmental structure typical of both the 40-kDa and 80-kDa actin-modulating proteins. Prominent similarities to the 80-kDa protein gelsolin especially exist with respect to the first segment and to the C-terminal segment. The comparatively high nucleation efficiency of the earthworm actin modulator is probably determined by its third segment which seems to enable the earthworm actin modulator to bind a second G-actin molecule more tightly than other previously described 40-kDa modulators.
Institut für Zoomorphologie und Zellbiologie, Heinrich-Heine-Universität Düsseldorf, Germany.
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T
Giebing
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Hinssen
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J
D'Haese
D000199:Actins / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites / Q000235:genetics; D003001:Cloning, Molecular; D003598:Cytoskeletal Proteins; D018076:DNA, Complementary / Q000235:genetics; D018260:Gelsolin / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009835:Oligochaeta / Q000235:genetics* / Q000378:metabolism; D016133:Polymerase Chain Reaction; D011506:Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D000199:Actins; D003598:Cytoskeletal Proteins; D018076:DNA, Complementary; D018260:Gelsolin; D011506:Proteins; C028514:actin-modulating proteins