A GELSOLIN-RELATED PROTEIN FROM LOBSTER MUSCLE - CLONING, SEQUENCE-ANALYSIS AND EXPRESSION

LUCK A, DHAESE J, Hinssen H (1995)
BIOCHEMICAL JOURNAL 305: 767-775.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
The tail muscle of the lobster Homarus americanus contains an actin-binding protein with an apparent molecular mass of 105 kDa determined by SDS/PAGE and gelsolin-like properties. We isolated this protein and peptide sequences were obtained after limited proteolysis with chymotrypsin. A tail-muscle-specific cDNA library was constructed in a lambda expression vector and a full-length clone was obtained by screening with a polyclonal anti(crustacean gelsolin) antibody. The cDNA insert of approx. 3.2 kb length was sequenced. The cDNA contained an open reading frame of 2.265 kb, and the deduced amino acid sequence of 754 residues (83 469 Da) identified the protein as a cytoplasmic member of the gelsolin/villin protein family. Comparison of the lobster gelsolin amino acid sequence with other members of this protein family revealed the characteristic 6-fold repeated segmental structure as well as the three conserved sequence motifs typical of each segment [Way and Weeds (1988) J. Mol. Biol. 203, 1127-1133]. Strong homologies were found with Drosophila gelsolin, human gelsolin, villin core, Dictyostelium severin and Physarum fragmin. In addition, the gelsolin-like protein from lobster muscle revealed motifs that were clearly similar to the actin-bundling region of human villin headpiece although it did not itself contain a distinct headpiece domain. The recombinant lobster gelsolin-like protein, expressed in Escherichia coli as a fusion protein, was purified from inclusion bodies and renatured as a functional protein. There were no significant differences in the biological activity tested between the recombinant and the native protein isolated from lobster muscle.
Erscheinungsjahr
Zeitschriftentitel
BIOCHEMICAL JOURNAL
Band
305
Seite
767-775
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LUCK A, DHAESE J, Hinssen H. A GELSOLIN-RELATED PROTEIN FROM LOBSTER MUSCLE - CLONING, SEQUENCE-ANALYSIS AND EXPRESSION. BIOCHEMICAL JOURNAL. 1995;305:767-775.
LUCK, A., DHAESE, J., & Hinssen, H. (1995). A GELSOLIN-RELATED PROTEIN FROM LOBSTER MUSCLE - CLONING, SEQUENCE-ANALYSIS AND EXPRESSION. BIOCHEMICAL JOURNAL, 305, 767-775.
LUCK, A., DHAESE, J., and Hinssen, H. (1995). A GELSOLIN-RELATED PROTEIN FROM LOBSTER MUSCLE - CLONING, SEQUENCE-ANALYSIS AND EXPRESSION. BIOCHEMICAL JOURNAL 305, 767-775.
LUCK, A., DHAESE, J., & Hinssen, H., 1995. A GELSOLIN-RELATED PROTEIN FROM LOBSTER MUSCLE - CLONING, SEQUENCE-ANALYSIS AND EXPRESSION. BIOCHEMICAL JOURNAL, 305, p 767-775.
A. LUCK, J. DHAESE, and H. Hinssen, “A GELSOLIN-RELATED PROTEIN FROM LOBSTER MUSCLE - CLONING, SEQUENCE-ANALYSIS AND EXPRESSION”, BIOCHEMICAL JOURNAL, vol. 305, 1995, pp. 767-775.
LUCK, A., DHAESE, J., Hinssen, H.: A GELSOLIN-RELATED PROTEIN FROM LOBSTER MUSCLE - CLONING, SEQUENCE-ANALYSIS AND EXPRESSION. BIOCHEMICAL JOURNAL. 305, 767-775 (1995).
LUCK, A, DHAESE, J, and Hinssen, Horst. “A GELSOLIN-RELATED PROTEIN FROM LOBSTER MUSCLE - CLONING, SEQUENCE-ANALYSIS AND EXPRESSION”. BIOCHEMICAL JOURNAL 305 (1995): 767-775.

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Langer M, Giebing T, D'Haese J., Comp Biochem Physiol B Biochem Mol Biol 119(4), 1998
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Multidomain structure and cellulosomal localization of the Clostridium thermocellum cellobiohydrolase CbhA.
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Murine adseverin (D5), a novel member of the gelsolin family, and murine adseverin are induced by interleukin-9 in T-helper lymphocytes.
Robbens J, Louahed J, De Pestel K, Van Colen I, Ampe C, Vandekerckhove J, Renauld JC., Mol Cell Biol 18(8), 1998
PMID: 9671468

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