Assimilatory sulfate reduction in C-3, C-3-C-4, and C-4 species of Flaveria

The activity of the enzymes catalyzing the first two steps of sulfate assim ilation, ATP sulfurylase and adenosine 5'-phosphosulfate reductase (APR), a re confined to bundle sheath cells in several C-4 monocot species. With the aim to analyze the molecular basis of this distribution and to determine w hether it was a prerequisite or a consequence of the C-4 photosynthetic mec hanism, we compared the intercellular distribution of the activity and the mRNA of APR in C-3, C-1-C-4, C-4-like, and C-4 species of the dicot genus F laveria. Measurements of APR activity, mRNA level, and protein accumulation in six Flaveria species revealed that APR activity, cysteine, and glutathi one levels were significantly higher in C-4-like and C-4 species than in C3 and C-3-C-4 species. ATP sulfurylase and APR mRNA were present at comparab le levels in both mesophyll and bundle sheath cells of C-4 species Flaveria trinervia. Immunogold electron microscopy demonstrated the presence of APR protein in chloroplasts of both cell types. These findings, taken together with results from the literature, show that the localization of assimilato ry sulfate reduction in the bundle sheath cells is not ubiquitous among C-4 plants and therefore is neither a prerequisite nor a consequence of C-4 ph otosynthesis.