Chloroplastic prenylated proteins.
By in vivo [3H]mevalonate labelling of spinach combined with biochemical analysis, evidence is provided for the existence of protein prenylation in chloroplasts. Approximately 20 prenylated polypeptides were resolved by SDS-PAGE followed by autoradiography. Thermolysin treatment of intact chloroplasts revealed that about 40% of the prenylated polypeptides were associated with the cytoplasmic surface of the outer envelope membrane. The remaining portion was present in thylakoids and/or the inner envelope membrane. The majority of the prenylated polypeptides were associated with larger membrane protein complexes. A farnesyl protein transferase activity was found to be associated with the thylakoid membrane.
Parmryd
I
I
Department of Biochemistry, Stockholm University, Sweden. ingela@biokemi.su.se
Shipton
C A
CA
Swiezewska
E
E
Dallner
G
G
Andersson
B
B
D019883:Alkyl and Aryl Transferases / Q000378:metabolism*; D002498:Centrifugation; D011232:Chemical Precipitation; D002736:Chloroplasts / Q000737:chemistry* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008798:Mevalonic Acid / Q000493:pharmacokinetics; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D017368:Protein Prenylation; D018724:Spinacia oleracea; D013347:Subcellular Fractions; D014316:Tritium
D008565:Membrane Proteins; D010940:Plant Proteins; D014316:Tritium; D019883:Alkyl and Aryl Transferases; C064911:p21(ras) farnesyl-protein transferase; D008798:Mevalonic Acid