THE COMPLETE SEQUENCE OF A 40-KDA ACTIN-MODULATING PROTEIN FROM THE EARTHWORM LUMBRICUS-TERRESTRIS

GIEBING T, Hinssen H, DHAESE J (1994)
EUROPEAN JOURNAL OF BIOCHEMISTRY 225(3): 773-779.

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Abstract
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.
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GIEBING T, Hinssen H, DHAESE J. THE COMPLETE SEQUENCE OF A 40-KDA ACTIN-MODULATING PROTEIN FROM THE EARTHWORM LUMBRICUS-TERRESTRIS. EUROPEAN JOURNAL OF BIOCHEMISTRY. 1994;225(3):773-779.
GIEBING, T., Hinssen, H., & DHAESE, J. (1994). THE COMPLETE SEQUENCE OF A 40-KDA ACTIN-MODULATING PROTEIN FROM THE EARTHWORM LUMBRICUS-TERRESTRIS. EUROPEAN JOURNAL OF BIOCHEMISTRY, 225(3), 773-779.
GIEBING, T., Hinssen, H., and DHAESE, J. (1994). THE COMPLETE SEQUENCE OF A 40-KDA ACTIN-MODULATING PROTEIN FROM THE EARTHWORM LUMBRICUS-TERRESTRIS. EUROPEAN JOURNAL OF BIOCHEMISTRY 225, 773-779.
GIEBING, T., Hinssen, H., & DHAESE, J., 1994. THE COMPLETE SEQUENCE OF A 40-KDA ACTIN-MODULATING PROTEIN FROM THE EARTHWORM LUMBRICUS-TERRESTRIS. EUROPEAN JOURNAL OF BIOCHEMISTRY, 225(3), p 773-779.
T. GIEBING, H. Hinssen, and J. DHAESE, “THE COMPLETE SEQUENCE OF A 40-KDA ACTIN-MODULATING PROTEIN FROM THE EARTHWORM LUMBRICUS-TERRESTRIS”, EUROPEAN JOURNAL OF BIOCHEMISTRY, vol. 225, 1994, pp. 773-779.
GIEBING, T., Hinssen, H., DHAESE, J.: THE COMPLETE SEQUENCE OF A 40-KDA ACTIN-MODULATING PROTEIN FROM THE EARTHWORM LUMBRICUS-TERRESTRIS. EUROPEAN JOURNAL OF BIOCHEMISTRY. 225, 773-779 (1994).
GIEBING, T, Hinssen, Horst, and DHAESE, J. “THE COMPLETE SEQUENCE OF A 40-KDA ACTIN-MODULATING PROTEIN FROM THE EARTHWORM LUMBRICUS-TERRESTRIS”. EUROPEAN JOURNAL OF BIOCHEMISTRY 225.3 (1994): 773-779.
This data publication is cited in the following publications:
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6 Citations in Europe PMC

Data provided by Europe PubMed Central.

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
Echinococcus granulosus: Cloning and Functional in Vitro Characterization of an Actin Filament Fragmenting Protein.
Cortez-Herrera E, Yamamoto RR, Rodrigues JJ, Farias SE, Ferreira HB, Zaha A., Exp. Parasitol. 97(4), 2001
PMID: 11384165
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
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
Molecular and mutational analysis of a gelsolin-family member encoded by the flightless I gene of Drosophila melanogaster.
de Couet HG, Fong KS, Weeds AG, McLaughlin PJ, Miklos GL., Genetics 141(3), 1995
PMID: 8582612

41 References

Data provided by Europe PubMed Central.

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

Meyer, Methods Enzymol. 201(), 1990
Muscle gelsolin: isolation from heart tissue and characterization as an integral myofibrillar protein.
Rouayrenc JF, Fattoum A, Gabrion J, Audemard E, Kassab R., FEBS Lett. 167(1), 1984
PMID: 6321238
Enzymatic amplification of beta-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia.
Saiki RK, Scharf S, Faloona F, Mullis KB, Horn GT, Erlich HA, Arnheim N., Science 230(4732), 1985
PMID: 2999980

Sambrook, 1989
DNA sequencing with chain-terminating inhibitors.
Sanger F, Nicklen S, Coulson AR., Proc. Natl. Acad. Sci. U.S.A. 74(12), 1977
PMID: 271968
Mechanism of interaction of Dictyostelium severin with actin filaments.
Yamamoto K, Pardee JD, Reidler J, Stryer L, Spudich JA., J. Cell Biol. 95(3), 1982
PMID: 6897549

Yin, Nature 281(), 1979

Yin, J. Cell Biol. 259(), 1985
Severin is a gelsolin prototype.
Yin HL, Janmey PA, Schleicher M., FEBS Lett. 264(1), 1990
PMID: 2159897

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