Dissection of Basal Body and Centriole Function in the Unicellular Green Alga Chlamydomonas reinhardtii

2005 ◽  
pp. 71-92
Author(s):  
Susan K. Dutcher
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Green Alga ◽  
Basal Body ◽  
Unicellular Green Alga

scholarly journals Asymmetric properties of the Chlamydomonas reinhardtii cytoskeleton direct rhodopsin photoreceptor localization

2011 ◽  
Vol 193 (4) ◽  
pp. 741-753 ◽  
Author(s):  
Telsa M. Mittelmeier ◽  
Joseph S. Boyd ◽  
Mary Rose Lamb ◽  
Carol L. Dieckmann
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Green Alga ◽  
Basal Body ◽  
Cytoskeletal Protein ◽  
Wild Type ◽  
Unicellular Green Alga ◽  
Protein Mutations ◽  
The Relationship ◽  
Mutant Cells ◽  
In Cells

The eyespot of the unicellular green alga Chlamydomonas reinhardtii is a photoreceptive organelle required for phototaxis. Relative to the anterior flagella, the eyespot is asymmetrically positioned adjacent to the daughter four-membered rootlet (D4), a unique bundle of acetylated microtubules extending from the daughter basal body toward the posterior of the cell. Here, we detail the relationship between the rhodopsin eyespot photoreceptor Channelrhodopsin 1 (ChR1) and acetylated microtubules. In wild-type cells, ChR1 was observed in an equatorial patch adjacent to D4 near the end of the acetylated microtubules and along the D4 rootlet. In cells with cytoskeletal protein mutations, supernumerary ChR1 patches remained adjacent to acetylated microtubules. In mlt1 (multieyed) mutant cells, supernumerary photoreceptor patches were not restricted to the D4 rootlet, and more anterior eyespots correlated with shorter acetylated microtubule rootlets. The data suggest a model in which photoreceptor localization is dependent on microtubule-based trafficking selective for the D4 rootlet, which is perturbed in mlt1 mutant cells.

scholarly journals Photosymbiose — neuartige Anwendungen in der Biomedizin

BIOspektrum ◽  
2021 ◽  
Vol 27 (2) ◽  
pp. 202-204
Author(s):  
Myra N. Chávez ◽  
Benedikt Fuchs ◽  
Jörg Nickelsen
Keyword(s):  
Tissue Engineering ◽  
Chlamydomonas Reinhardtii ◽  
Green Alga ◽  
Recombinant Proteins ◽  
Biomedical Devices ◽  
Unicellular Green Alga ◽  
Surgical Sutures ◽  
Novel Strategy ◽  
Clinical Problems

AbstractWe have recently proposed a novel strategy named photosynthetic tissue engineering to overcome clinical problems due to hypoxia. The idea is based on transgenic photoautotrophic microorganisms that produce oxygen and at the same time secrete functional recombinant proteins into tissues. In particular, the unicellular green alga Chlamydomonas reinhardtii has successfully been used to boost the regenerative potential of several biomedical devices, such as dermal scaffolds and surgical sutures.

scholarly journals Crystal structure of chloroplast fructose-1,6-bisphosphate aldolase from the green alga Chlamydomonas reinhardtii

2021 ◽  
Author(s):  
Théo Le Moigne ◽  
Edoardo Sarti ◽  
Antonin Nourisson ◽  
Alessandra Carbone ◽  
Stéphane D. Lemaire ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Chlamydomonas Reinhardtii ◽  
Green Alga ◽  
Distinct Group ◽  
Multiple Sequence ◽  
Post Translational Modifications ◽  
Photosynthetic Organisms ◽  
Unicellular Green Alga ◽  
Tim Barrel ◽  
Fructose 1,6 Bisphosphate

The Calvin-Benson cycle fixes carbon dioxide into organic triosephosphates through the collective action of eleven conserved enzymes. Regeneration of ribulose-1,5-bisphosphate, the substrate of Rubisco-mediated carboxylation, requires two lyase reactions catalyzed by fructose-1,6-bisphosphate aldolase (FBA). While cytoplasmic FBA has been extensively studied in non-photosynthetic organisms, functional and structural details are limited for chloroplast FBA encoded by oxygenic phototrophs . Here we determined the crystal structure of plastidial FBA from the unicellular green alga Chlamydomonas reinhardtii (Cr). We confirm that CrFBA folds as a TIM barrel, describe its catalytic pocket and homo-tetrameric state. Multiple sequence profiling classified the photosynthetic paralogs of FBA in a distinct group from non-photosynthetic paralogs. We mapped the sites of thiol- and phospho-based post-translational modifications known from photosynthetic organisms and predict their effects on enzyme catalysis.

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