The Unicellular Green Alga Chlamydomonas reinhardtii as an Experimental System to Study Chloroplast RNA Metabolism

2000 ◽  
Vol 87 (3) ◽  
pp. 97-107 ◽  
Author(s):  
J. Nickelsen ◽  
U. Kück
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Green Alga ◽  
Experimental System ◽  
Rna Metabolism ◽  
Unicellular Green Alga ◽  
Chloroplast Rna

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.

Use of plant chloroplast RNA-binding proteins as orthogonal activators of chloroplast transgenes in the green alga Chlamydomonas reinhardtii

2021 ◽  
Vol 60 ◽  
pp. 102535
Author(s):  
Noam Shahar ◽  
Tamar Elman ◽  
Rosalind Williams-Carrier ◽  
Oren Ben-Zvi ◽  
Iftach Yacoby ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Green Alga ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Plant Chloroplast ◽  
Chloroplast Rna

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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