Schoenitzer, Veronika and Eichner, Norbert and Clausen-Schaumann, Hauke and Weiss, Ingrid M. (2011) Transmembrane myosin chitin synthase involved in mollusc shell formation produced in Dictyostelium is active. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 415 (4). pp. 586-590. ISSN 0006-291X,
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Several mollusc shells contain chitin, which is formed by a transmembrane myosin motor enzyme. This protein could be involved in sensing mechanical and structural changes of the forming, mineralizing extracellular matrix. Here we report the heterologous expression of the transmembrane myosin chitin synthase Ar-CS1 of the bivalve mollusc Atrina rigida (2286 amino acid residues, M.W. 264 kDa/monomer) in Dictyostelium discoideum, a model organism for myosin motor proteins. Confocal laser scanning immunofluorescence microscopy (CLSM), chitin binding GFP detection of chitin on cells and released to the cell culture medium, and a radiochemical activity assay of membrane extracts revealed expression and enzymatic activity of the mollusc chitin synthase in transgenic slime mold cells. First high-resolution atomic force microscopy (AFM) images of Ar-CS1 transformed cellulose synthase deficient D. discoideum dcsA(-) cell lines are shown. (C) 2011 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PLASMA-MEMBRANE; LARVAL SHELLS; DISCOIDEUM; GENE; EXPRESSION; PROTEINS; HEAD; Biomineralization; Chitin; Dictyostelium; Glycosyltransferase; Transmembrane myosin ATPase |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 25 May 2020 13:01 |
| Last Modified: | 25 May 2020 13:01 |
| URI: | https://pred.uni-regensburg.de/id/eprint/19682 |
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