Fischer, Harald and Robl, Ingrid and Sumper, Manfred and Kroeger, Nils (1999) Targeting and covalent modification of cell wall and membrane proteins heterologously expressed in the diatom Cylindrotheca fusiformis (Bacillariophyceae). JOURNAL OF PHYCOLOGY, 35 (1). pp. 113-120. ISSN 0022-3646,
Full text not available from this repository.Abstract
Diatoms are unicellular organisms encased by silica-based cell walls that display species-specific structures, Morphogenesis of diatom cell walls is believed to be controlled by a polysaccharide/protein-matrix that remains associated with mature cell walls, Recently, a family of calcium-binding glycoproteins, the frustulins, has been identified as major diatom cell wall component, Here we describe a transformation-based approach to investigate intracellular targeting and function of frustulins, When epsilon-frustulin from the diatom Navicula pelliculosa is expressed in Cylindrotheca fusiformis, it is correctly targeted into the cell wall, Furthermore, the unique N-terminus of epsilon-frustulin was properly modified, indicating that C. fusiformis and N. pelliculosa contain homologous fi frustulin-processing proteases, In a different transformation experiment, a modified version of the Chlorella kessleri hexose/H+ symporter bearing a bacterial biotinyl-acceptor domain was expressed in C, fusiformis. The transporter became biotinylated in vivo and was functionally incorporated into the plasma membrane, allowing C. fusiformis to take up C-14-glucose and C-14-glucosamine. Stage-specific radioactive labeling with this transformant revealed that secretion of frustulins is strongly enhanced during cell wall development, The data presented in this study demonstrate for the first time functional expression of a membrane protein and correct targeting of a cell wall protein heterologously expressed in a diatom cell.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | GENE; TRANSFORMATION; FAMILY; SYMPORTER; Bacillariophyceae; biotinylation; cell wall; Cylindrotheca fusiformis; metabolic labeling; protein targeting; transformation |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Pflanzenwissenschaften > Lehrstuhl für Zellbiologie und Pflanzenphysiologie (Prof. Dr. Klaus Grasser) Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 22 Nov 2022 11:49 |
| Last Modified: | 22 Nov 2022 11:49 |
| URI: | https://pred.uni-regensburg.de/id/eprint/48555 |
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