Chloroplast intragenic suppression enhances the low CO2/O2 specificity of mutant ribulose-bisphosphate carboxylase/oxygenase.

The competition between CO2 and O2 at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase limits net CO2 fixation in photosynthesis. In the green alga Chlamydomonas reinhardtii, a mutation in the chloroplast large-subunit gene reduces the CO2/O2 specificity of the enzyme by 37% and causes valine-331 to be replaced by alanine. Revertant selection identified an intragenic suppressor mutation that increases the CO2/O2 specificity of the mutant enzyme by 33%. This second-site mutation causes threonine-342 to be replaced by isoleucine. The complementing amino acid substitutions flank a catalytically essential lysyl residue at position 334. It thus appears that a number of amino acid residues can influence the CO2/O2 specificity of this bifunctional enzyme. The well defined chloroplast genetics of C. reinhardtii allows the interactions of these residues to be investigated.

• Publication year

  1989

• Venue

  Journal of Biological Chemistry

• Publication date

  1989-02-25

• Fields of study

  Biology, Medicine, Environmental Science

• Identifiers
  DOI 10.1016/s0021-9258(18)94027-5PMID 2492528
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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