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PMID: 16659874 Published · ppublish English Journal Article

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

Plant physiology ·Vol. 59 ·No. 3 ·1977-03-00 ·Pages 464-70

Howell SH, Heizmann P, Gelvin S, Walker LL

Abstract

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.

Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Howell S H
Department of Biology, University of California, San Diego, La Jolla, California 92093.
Heizmann P
Gelvin S
Walker L L
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Article Info
Journal
Plant physiology
Abbr.
Plant Physiol
ISSN
0032-0889
DOI
10.1104/pp.59.3.464
Published
1977-03-00
Pages
464-70
Language
English
Region
United States
NLM ID
0401224
PMCID
PMC542425
External Links
PubMed source DOI: 10.1104/pp.59.3.464 PMC Full Text View journal details
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