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. 1970 Mar 1;44(3):531–539. doi: 10.1083/jcb.44.3.531

CHLOROPLAST STRUCTURE AND FUNCTION IN ac-20, A MUTANT STRAIN OF CHLAMYDOMONAS REINHARDI

I. CO2 Fixation and Ribulose-1,5-Diphosphate Carboxylase Synthesis

R K Togasaki 1, R P Levine 1
PMCID: PMC2107964  PMID: 4984375

Abstract

A mutant strain of the green alga Chlamydomonas reinhardi, ac-20, is described in which both the rate of CO2 fixation by whole cells and the rate of carboxylation of ribulose-1,5-diphosphate in cell-free extracts are reduced, particularly when sodium acetate is present in the growth medium. Of the enzymes of the reductive pentose phosphate cycle tested, only ribulose-1,5-diphosphate carboxylase activity is reduced in the mutant strain, and it appears that the low carboxylase activity limits the strain's rate of photosynthetic carbon metabolism. Evidence is presented to show that the fluctuation in the level of the enzyme activity in the presence or absence of acetate results from the fluctuation in the level of some factor(s) limiting the rate of synthesis of the protein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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