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Ribulose bisphosphate carboxylase in algae: synthesis, enzymology and evolution.
1Department of Botany, University of Washington, 98195, Seattle, WA, USA.
Photosynthesis Research
|January 15, 2014
Summary
Differences in algal ribulose-1,5-bisphosphate carboxylase (Rubisco) enzymes highlight evolutionary history. These variations in structure and function offer insights into the origin and diversification of algal plastids.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Chloroplast structure and biochemistry studies inform hypotheses on algal plastid origins.
- Ribulose-1,5-bisphosphate carboxylase (Rubisco) exhibits significant variation across eukaryotic algal supertaxa.
Purpose of the Study:
- To investigate variations in Rubisco structure and function across different algal taxa.
- To correlate these variations with the evolutionary history of algal plastids.
Main Methods:
- Comparative genetic and biochemical analyses of Rubisco.
- Examination of gene location, arrangement, synthesis, and polypeptide characteristics.
- Assessment of substrate binding, inhibitor action, and enzyme kinetics.
Main Results:
- Chromophytic and rhodophytic Rubisco share similarities in substrate/inhibitor binding and polypeptide sequence.
- Chlorophytes, prokaryotes, and chromophytes/rhodophytes display distinct enzyme kinetics and subunit structures.
- Chlorophytic small subunit polypeptides show variability, unlike conserved versions in chromophytes and rhodophytes.
Conclusions:
- Taxa-specific Rubisco differences reflect plastid evolutionary history and functional requirements.
- Gene encoding location (organelle) influences Rubisco evolution.
- Comparative Rubisco analysis provides insights into algal diversification.
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