Plant Physiol.
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Plant Physiology 59:464-470 (1977)
© 1977 American Society of Plant Biologists

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Articles

Identification and Properties of the Messenger RNA Activity in Chlamydomonas reinhardi Coding for the Large Subunit of D-ribulose-1,5-bisphosphate Carboxylase 1

Stephen H. Howell, Philippe Heizmann2, Stanton Gelvin and Linda L. Walker

a Department of Biology, University of California, San Diego, La Jolla, California 92093

Properties of the mRNA coding for the large subunit of ribulose-1,5-bisphosphate carboxylase from Chlamydomonas reinhardi were determined. Large subunit synthesis, directed by RNA from partially purified whole cell extracts, was detected by specific immunoprecipitation of polypeptide products synthesized in a heterologous translation system derived from Escherichia coli. Large subunit synthesis showed sharp RNA concentration dependence in an E. coli translation system, and at optimal RNA concentrations, immunoprecipitable large subunit synthesis accounted for 2% of the total incorporation. Large subunit messenger activity sedimented at 12 to 14S on nondenaturing sucrose gradients and did not bind to oligo(dT)-cellulose suggesting the mRNA is not polyadenylated. The immunoprecipitable products translated in vitro are not complete polypeptide chains, but are smaller peptides identifiable as large subunit fragments by tryptic fingerprint analysis. No immunoprecipitable product was obtained when similar RNA fractions were tested in a wheat germ translation system.

2 Permanent address: Départment de Biologie Générale et Appliquée, Laboratoire associé ou CNRS, Université Lyon I, 69 Villeurbanne, France.

1 This work was supported by National Science Foundation Grant BMS 75-0500. P. H. is a recipient of a NATO research award, and S. G. is supported by United States Public Health Service Training Grant GM 00702-15.






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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1977 by the American Society of Plant Biologists