Acclimation to low [CO2] by an inorganic carbon-concentrating mechanism in Cyanophora paradoxa

S. C. Burey, V. Poroyko, Z. N. Ergen, S. Fathi-Nejad, C. Schüller, N. Ohnishi, H. Fukuzawa, H. J. Bohnert, W. Löffelhardt

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)


The glaucocystophyte Cyanophora paradoxa contains cyanelles, plastids with prokaroytic features such as a peptidoglycan wall and a central proteinaceous inclusion body. While this central body includes the majority of the enzyme ribulose 1,5-bisphosphate carboxylase/oxgenase Rubisco), the presence of a carbon-concentrating mechanism (CCM) in C. paradoxa has only been hypothesized. Here, we present physiological data in support of a CCM: CO2 exchange activity as well as apparent affinity against inorganic carbon were found to increase under CO2-limiting stress. Further, expressed sequence tags (ESTs) of C. paradoxa were obtained from two cDNA libraries, one from cells grown in high [CO2] conditions and one from cells grown under low [CO2] conditions. A cDNA microarray platform assembled from 2378 cDNA sequences revealed that 142 genes significantly responded to a shift from high to low [CO2]. Trends in gene expression were comparable to those reported for Chlamydomonas reinhardtii and the cyanobacterium Synechocystis 6803, both possessing a CCM. Among genes regulated by [CO2], transcripts were identified encoding carbonic anhydrases (CAs), Rubisco activase and a putative bicarbonate transporter in C. paradoxa, likely functionally involved in the CCM. These results and the polyhedric appearance of the central body further support the hypothesis of a unique 'eukaryotic carboxysome' in Cyanophora.

Original languageEnglish
Pages (from-to)1422-1435
Number of pages14
JournalPlant, Cell and Environment
Issue number11
Publication statusPublished - Nov 2007
Externally publishedYes


  • Carboxysome
  • Cyanelle
  • Microarrays
  • cDNA library

ASJC Scopus subject areas

  • Physiology
  • Plant Science


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