scholarly journals Cyanophora paradoxa mitochondrial tRNAs play a double game

2021 ◽  
Author(s):  
Thalia Salinas‐Giegé ◽  
Elodie Ubrig ◽  
Laurence Drouard
Keyword(s):  
Cyanophora Paradoxa

Cytochrome c6 from Cyanophora paradoxa . Characterization of the protein and the cDNA of the precursor and import into isolated cyanelles

2000 ◽  
Vol 267 (13) ◽  
pp. 4232-4241 ◽  
Author(s):  
Jurgen M. Steiner ◽  
Aurelio Serrano ◽  
Gunter Allmaier ◽  
Johannes Jakowitsch ◽  
Wolfgang Loffelhardt
Keyword(s):  
Cyanophora Paradoxa ◽  
Cytochrome C6

Analysis of the Genome of Cyanophora paradoxa: An Algal Model for Understanding Primary Endosymbiosis

Endosymbiosis ◽  
2013 ◽  
pp. 135-148 ◽  
Author(s):  
Debashish Bhattacharya ◽  
Dana C. Price ◽  
Cheong Xin Chan ◽  
Jeferson Gross ◽  
Jürgen M. Steiner ◽  
...  
Keyword(s):  
Cyanophora Paradoxa ◽  
Primary Endosymbiosis

Protein Translocation into and within an Armoured Plastid: The Cyanelle of Cyanophora Paradoxa

1998 ◽  
pp. 3057-3061 ◽  
Author(s):  
Wolfgang Löffelhardt ◽  
Jürgen Steiner ◽  
Yan Ma ◽  
Johannes Jakowitsch
Keyword(s):  
Protein Translocation ◽  
Cyanophora Paradoxa

Der einflub von cycloheximid und chloramphenicol auf die biosynthese der photosynthese-pigmente in cyanophora paradoxa korsch. III. chlorophyll a und phycochromoproteide / The influence of cycloheximide and chloramphenicol on the biosynthesis of the photosvnthetic pigments in cyanophora paradoxa. III. chlorophyll a and phycochromoproteids

1983 ◽  
Vol 38 (11-12) ◽  
pp. 990-995 ◽  
Author(s):  
Margarete Neu-Müller ◽  
Hainfried E. A. Schenk
Keyword(s):  
Chlorophyll A ◽  
Cyanophora Paradoxa ◽  
Inhibition Effect ◽  
Vis Spectroscopy ◽  
Chl Biosynthesis ◽  
Better Than

The inhibition effects of CHI and CA on the biosynthesis of the tetrapyrrolpigments were measured with two methods (in vivo VIS-spectroscopy, for chlorophyll (Chi) and the phycochromoproteids, 14C incorporation only for Chi). In the case of the Chl-biosynthesis both methods show the same results: a) In vivo VIS-spectroscopy demonstrates that the inhibition effect of CA manifests faster than that of CHI, b) during the 14C incorporation into Chi chloramphenicol (CA) inhibits more than cyclohexim ide (CHI) in contrary to the behaviour of chloroplasts. It seems that the CHI caused decrease of 14C incorporation into Chi can be ascribed to the decreased photosynthesis. The influence o f the antibiotics of the phycochrom oproteids is similar to that observed for chlorophyll. It is remarkable that under the influence of CHI the phycochromoproteid biosynthesis is significantly better than under CA influence, although CHI damages the consortium more than CA. That can be interpreted, as for chlorophyll, with a more endocytobiont coded phycochrom oproteid synthesis

Analysis of Cyanophora paradoxa tells important lessons on plastid evolution

2015 ◽  
Vol 2 (1) ◽  
pp. 3-10 ◽  
Author(s):  
Fabio Facchinelli ◽  
Andreas P. M. Weber
Keyword(s):  
Cyanophora Paradoxa ◽  
Plastid Evolution

The Phycobihproteids in Cyanophora paradoxa as Accessoric Pigments and Nitrogen Storage Proteins

1983 ◽  
Vol 38 (11-12) ◽  
pp. 972-977 ◽  
Author(s):  
Hainfried E. A. Schenk ◽  
Jürgen Hanf ◽  
Margarete Neu-Müller
Keyword(s):  
Electron Transport ◽  
Stress Proteins ◽  
Nitrogen Starvation ◽  
Storage Proteins ◽  
Photosynthetic Electron Transport ◽  
Lower Degree ◽  
Nitrogen Storage ◽  
Cyanophora Paradoxa ◽  
Free Living

The phycobiliproteids of cyanobacteria have two functions. They are accessoric pigments for the light-dependent photosynthetic electron transport, and, secondly, they are storage proteins. Cyanocyta korschikoffiana, the endocyanelle of Cyanophora paradoxa, a hardly adapted endocytobiotic cyanobacterium, is responsible for the photoautotrophy of the host flagellate. The biosynthesis of the phycobiliproteids takes place in the endocyanelles and is reversible. Under nitrogen starvation the phycobiliproteids were disintegrated again, in contrast to the carotenoids (and in a lower degree to chlorophyll), whose contents rem ain more constant in the cells, as shown by in vivo measurements. Therefore, it is concluded that sim ilar to the function in free living cyanobacteria the phycobiliproteids of C. paradoxa also serve as storage substances (“stress proteins”). This opinion is supported by experiments with chloramphenicol

CpKLP1: A CALMODULIN-BINDING KINESIN-LIKE PROTEIN FROM CYANOPHORA PARADOXA (GLAUCOPHYTA)

2000 ◽  
Vol 36 (4) ◽  
pp. 686-692 ◽  
Author(s):  
Salah E. Abdel-Ghany ◽  
Paul Kugrens ◽  
A. S. N. Reddy
Keyword(s):  
Cyanophora Paradoxa ◽  
Calmodulin Binding
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