Protein synthesis in chloroplasts. IV. Polypeptides of the chloroplast envelope.
Envelope membranes were isolated from washed chloroplasts of pea seedlings. As judged by the protein-to-chlorophyll ratio, average preparations contain less than 8 percent contamination with internal lamellar membranes. Electrophoresis on sodium dodecylsulphate polyacrylamide gels shows that the envelope membranes contain at least 25 polypeptides. The molecular weight distribution of the envelope polypeptides is different from that of the lamellar polypeptides, there being more polypeptides of molecular weights above 50 000 in the envelopes. Two envelope polypeptides become labelled when isolated intact chloroplasts are incubated in the light with (35S) methionine. One of these is similar in molecular weight to the main polypeptide labelled in lamellae, but the other is unique to the envelope fraction. Incorporation of label into both polypeptides is totally light-dependent and is inhibited by chloramphenicol. When (35S) methionine is fed to detached pea shoots with and without cycloheximide, the labelling of other envelope polypeptides is inhibited. We conclude that two polypeptides of the chloroplast envelop are synthesised by chloroplast ribosomes.
D002462:Cell Membrane / Q000378:metabolism; D002701:Chloramphenicol / Q000494:pharmacology; D002736:Chloroplasts / Q000187:drug effects / Q000378:metabolism* / Q000648:ultrastructure; D003513:Cycloheximide / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D008715:Methionine / Q000378:metabolism; D008970:Molecular Weight; D010452:Peptide Biosynthesis; D010940:Plant Proteins / Q000096:biosynthesis*; D010944:Plants; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism
D010940:Plant Proteins; D002701:Chloramphenicol; D003513:Cycloheximide; D008715:Methionine