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.
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BIOCHEMICAL JOURNAL
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305
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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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Four paralog gelsolin genes are differentially expressed in the earthworm Lumbricus terrestris.
Thiruketheeswaran P, Thomalla P, Krüger E, Hinssen H, D'Haese J., Comp Biochem Physiol B Biochem Mol Biol 208-209(), 2017
PMID: 28400331
Isoforms of gelsolin from lobster striated muscles differ in calcium-dependence.
Unger A, Brunne B, Hinssen H., Arch Biochem Biophys 536(1), 2013
PMID: 23707758
Electron-microscopical localization of gelsolin in various crustacean muscles.
Unger A, Hinssen H., Cell Tissue Res 341(2), 2010
PMID: 20607291
Der f 16: a novel gelsolin-related molecule identified as an allergen from the house dust mite, Dermatophagoides farinae.
Kawamoto S, Suzuki T, Aki T, Katsutani T, Tsuboi S, Shigeta S, Ono K., FEBS Lett 516(1-3), 2002
PMID: 11959139
Purification and functional characterization of an 85-kDa gelsolin from the ascidians Microcosmus sulcatus and Phallusia mammilata.
Langer M, Giebing T, D'Haese J., Comp Biochem Physiol B Biochem Mol Biol 119(4), 1998
PMID: 9787761
Multidomain structure and cellulosomal localization of the Clostridium thermocellum cellobiohydrolase CbhA.
Zverlov VV, Velikodvorskaya GV, Schwarz WH, Bronnenmeier K, Kellermann J, Staudenbauer WL., J Bacteriol 180(12), 1998
PMID: 9620957
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

48 References

Daten bereitgestellt von Europe PubMed Central.

Identification of secreted and cytosolic gelsolin in Drosophila.
Stella MC, Schauerte H, Straub KL, Leptin M., J. Cell Biol. 125(3), 1994
PMID: 8175883
The 100 kDa F-actin capping protein of Dictyostelium amoebae is a villin prototype ('protovillin').
Hofmann A, Noegel AA, Bomblies L, Lottspeich F, Schleicher M., FEBS Lett. 328(1-2), 1993
PMID: 8344435
Structure of gelsolin segment 1-actin complex and the mechanism of filament severing.
McLaughlin PJ, Gooch JT, Mannherz HG, Weeds AG., Nature 364(6439), 1993
PMID: 8395021
Cloning of a secretory gelsolin from Drosophila melanogaster.
Heintzelman MB, Frankel SA, Artavanis-Tsakonas S, Mooseker MS., J. Mol. Biol. 230(3), 1993
PMID: 8386771
Cap100, a novel phosphatidylinositol 4,5-bisphosphate-regulated protein that caps actin filaments but does not nucleate actin assembly.
Hofmann A, Eichinger L, Andre E, Rieger D, Schleicher M., Cell Motil. Cytoskeleton 23(2), 1992
PMID: 1333365
Phosphoinositide-binding peptides derived from the sequences of gelsolin and villin.
Janmey PA, Lamb J, Allen PG, Matsudaira PT., J. Biol. Chem. 267(17), 1992
PMID: 1318302
In vivo analysis of functional domains from villin and gelsolin.
Finidori J, Friederich E, Kwiatkowski DJ, Louvard D., J. Cell Biol. 116(5), 1992
PMID: 1310994
Are the conserved sequences in segment 1 of gelsolin important for binding actin?
Way M, Pope B, Weeds AG., J. Cell Biol. 116(5), 1992
PMID: 1310993
An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin.
Friederich E, Vancompernolle K, Huet C, Goethals M, Finidori J, Vandekerckhove J, Louvard D., Cell 70(1), 1992
PMID: 1623524
Distribution of a gelsolin-like 74,000 mol. wt protein in neural and endocrine tissues.
Sakurai T, Ohmi K, Kurokawa H, Nonomura Y., Neuroscience 38(3), 1990
PMID: 2176721
Identification of critical functional and regulatory domains in gelsolin.
Kwiatkowski DJ, Janmey PA, Yin HL., J. Cell Biol. 108(5), 1989
PMID: 2541138
Villin sequence and peptide map identify six homologous domains.
Bazari WL, Matsudaira P, Wallek M, Smeal T, Jakes R, Ahmed Y., Proc. Natl. Acad. Sci. U.S.A. 85(14), 1988
PMID: 2839826
Gelsolin has three actin-binding sites.
Bryan J., J. Cell Biol. 106(5), 1988
PMID: 2836434
Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains.
Andre E, Lottspeich F, Schleicher M, Noegel A., J. Biol. Chem. 263(2), 1988
PMID: 2826459
Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity.
Arpin M, Pringault E, Finidori J, Garcia A, Jeltsch JM, Vandekerckhove J, Louvard D., J. Cell Biol. 107(5), 1988
PMID: 2846586
Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain.
Kwiatkowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, Yin HL., Nature 323(6087), 1986
PMID: 3020431
Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate.
Janmey PA, Stossel TP., Nature 325(6102), 1987
PMID: 3027569
Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking.
Janmey PA, Chaponnier C, Lind SE, Zaner KS, Stossel TP, Yin HL., Biochemistry 24(14), 1985
PMID: 2994715
Can villin be used to identify malignant and undifferentiated normal digestive epithelial cells?
Robine S, Huet C, Moll R, Sahuquillo-Merino C, Coudrier E, Zweibaum A, Louvard D., Proc. Natl. Acad. Sci. U.S.A. 82(24), 1985
PMID: 3909146
Actin-gelsolin interactions. Evidence for two actin-binding sites.
Bryan J, Kurth MC., J. Biol. Chem. 259(12), 1984
PMID: 6330060
A Ca2+-dependent actin modulator from vertebrate smooth muscle.
Hinssen H, Small JV, Sobieszek A., FEBS Lett. 166(1), 1984
PMID: 6537923
Calcium control of the intestinal microvillus cytoskeleton: its implications for the regulation of microfilament organizations.
Glenney JR Jr, Bretscher A, Weber K., Proc. Natl. Acad. Sci. U.S.A. 77(11), 1980
PMID: 6935660
Fragmin: a calcium ion sensitive regulatory factor on the formation of actin filaments.
Hasegawa T, Takahashi S, Hayashi H, Hatano S., Biochemistry 19(12), 1980
PMID: 6893158
Villin: the major microfilament-associated protein of the intestinal microvillus.
Bretscher A, Weber K., Proc. Natl. Acad. Sci. U.S.A. 76(5), 1979
PMID: 287075
DNA sequencing with chain-terminating inhibitors.
Sanger F, Nicklen S, Coulson AR., Proc. Natl. Acad. Sci. U.S.A. 74(12), 1977
PMID: 271968

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