Differential expression of ribulose-1,5-bisphosphate carboxylase in reciprocal F1 hybrids of a C3 and a C4-like Flaveria species.

Stable reciprocal hybrids between Flaveria pringlei (C3) and F. brownii (C4-like) have been produced by standard breeding techniques. There are no differences in the isoelectric focusing patterns of the catalytic subunits of the ribulose-1,5-bisphosphate carboxylase/oxygenase from F. pringlei, F. brownii, or the reciprocal hybrids. The enzyme from both species also contains an identical noncatalytic subunit polypeptide. However, the carboxylase enzyme from F. brownii contains another isomeric form of noncatalytic subunit polypeptide which is resolveable by isoelectric focusing. This isomeric form constitutes about 50% of the total noncatalytic subunits in this species. It comprises only about 10% of the total noncatalytic subunit population in the C3 x C4 plants, but about 42% of the noncatalytic subunits in the reciprocal cross. The concentrations of the holoenzyme in the reciprocal hybrids are comparable to those of the respective maternal parent. We hypothesize that a differential inheritance of parental chloroplasts by the reciprocal hybrids may be associated with this apparent maternal influence on the expression of the noncatalytic polypeptides and the holoenzyme concentration.