Fuhrmann, Markus and Stahlberg, A. and Govorunova, E. and Rank, S. and Hegemann, P. (2001) The abundant retinal protein of the Chlamydomonas eye is not the photoreceptor for phototaxis and photophobic responses. JOURNAL OF CELL SCIENCE, 114 (21). pp. 3857-3863. ISSN 0021-9533
Full text not available from this repository. (Request a copy)Abstract
The chlamyopsin gene (cop) encodes the most abundant eyespot protein in the unicellular green alga Chlamydomonas reinhardtii. This opsin-related protein (COP) binds retinal and was thought to be the photoreceptor controlling photomovement responses via a set of photoreceptor currents. Unfortunately, opsin-deficient mutants are not available and targeted disruption of non-selectable nuclear genes is not yet possible in any green alga. Here we show that intron-containing gene fragments directly linked to their intron-less antisense counterpart provide efficient post-transcriptional gene silencing (PTGS) in C. reinhardtii, thus allowing an efficient reduction of a specific gene product in a green alga. In opsin-deprived transformants, Hash-induced photoreceptor currents (PC) are left unchanged. Moreover, photophobic responses as studied by motion analysis and phototaxis tested in a light-scattering assay were indistinguishable from the responses of untransformed wild-type cells. We conclude that phototaxis and photophobic responses in C. reinhardtii are triggered by an as yet unidentified rhodopsin species.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ALGA VOLVOX-CARTERI; MESSENGER-RNA DEGRADATION; DOUBLE-STRANDED-RNA; GREEN-ALGA; HOMOLOGOUS RECOMBINATION; SENSORY PHOTORECEPTOR; GENE-EXPRESSION; REINHARDTII; RHODOPSIN; LIGHT; RNAi; chlamyopsin; antisense |
| 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: | 30 Nov 2021 10:33 |
| Last Modified: | 30 Nov 2021 10:33 |
| URI: | https://pred.uni-regensburg.de/id/eprint/40977 |
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