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Rubisco rules fall; gene transfer triumphs

J D Palmer1

  • 1Department of Biology, Indiana University, Bloomington 47405, USA.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology
|December 1, 1995
PubMed
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Dinoflagellate plastids utilize a form II Rubisco enzyme, typically found in anaerobic bacteria, instead of the usual form I. This discovery challenges our understanding of carbon fixation in aerobic organisms and highlights extensive gene transfer in enzyme evolution.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) is a key CO2-fixing enzyme, predominantly Form I in oxygenic phototrophs.
  • Form II Rubisco was previously known only in anaerobic proteobacteria.

Purpose of the Study:

  • To investigate the unusual presence of Form II Rubisco in dinoflagellate plastids.
  • To explore the implications of this enzyme substitution for aerobic carbon fixation.
  • To characterize the unique molecular properties of dinoflagellate Rubisco.

Main Methods:

  • Comparative genomics and phylogenetic analysis of Rubisco genes.
  • Molecular characterization of dinoflagellate Rubisco structure and function.

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Main Results:

  • Dinoflagellate plastids contain Form II Rubisco, not the expected Form I.
  • Dinoflagellate Rubisco genes are nuclear-encoded, produce polyproteins, and contain noncanonical introns.
  • These genes exhibit alpha-proteobacterial origins, suggesting lateral gene transfer.

Conclusions:

  • The presence of oxygen-sensitive Form II Rubisco in aerobic dinoflagellates raises questions about its functional adaptation.
  • Nuclear encoding and unusual gene features suggest a possible mitochondrial origin for dinoflagellate Rubisco.
  • This finding underscores the significant role of lateral gene transfer in the evolution of essential metabolic enzymes like Rubisco.