Biochemical Genetics

, Volume 27, Issue 9–10, pp 497–505 | Cite as

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

  • Sarjit Johal
  • A. Scott Holaday
Article
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Revised:

Abstract

Stable reciprocal hybrids betweenFlaveria pringlei (C3) andF. 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 fromF. pringlei, F. brownii, or the reciprocal hybrids. The enzyme from both species also contains an identical noncatalytic subunit polypeptide. However, the carboxylase enzyme fromF. 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×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.

Key words

ribulose-1,5-bisphosphate carboxylase/oxygenase C3 C4 Flaveria 
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Copyright information

© Plenum Publishing Corporation 1989

Authors and Affiliations

  • Sarjit Johal
    • 1
  • A. Scott Holaday
    • 2
  1. 1.BP America, Research and DevelopmentCleveland
  2. 2.Department of Biological SciencesTexas Tech UniversityLubbock

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