Related Experiment Video
Updated: Aug 9, 2026

mRNA Interactome Capture from Plant Protoplasts
Published on: July 28, 2017
Translation of mRNAs for subunits of chloroplast coupling factor 1 in spinach
1Waksman Institute of Microbiology, Rutgers University, Piscataway, New Jersey 08854.
Abstract:
The chloroplast coupling factor 1 consists of five nonidentical subunits, three of which (alpha, beta, and epsilon subunits) have been shown in several laboratories to be synthesized within chloroplasts. The site of synthesis of the remaining two (gamma and delta subunits) was investigated by analyzing products directed by spinach leaf RNAs in wheat germ and reticulocyte translation systems in vitro. It was found that poly(A)(+) RNA directs the synthesis of two distinct polypeptides, one of which is immunochemically related to the gamma subunit but is 4,000 daltons larger. The other shares antigenic sites with the delta subunit but is 8,000 daltons larger. When wheat germ or reticulocyte translation systems were programmed with RNAs from purified chloroplasts, the only products related to CF(1) that we could detect were a putative precursor of beta, 2,000 daltons larger than the mature subunit, and some smaller polypeptides, which appear to be incomplete translation products of beta. From these results it appears likely that the gamma and delta subunits are synthesized in the cytoplasm as larger precursors and that beta is synthesized within the chloroplast as a precursor.
Related Concept Videos
Protein Transport to the Stroma
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
Protein Transport to the Inner Chloroplast Membrane
Riboswitches
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
Translation in Prokaryotes
Protein Transport to the Outer Chloroplast Membrane
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
Regulated mRNA Transport

