Proteins are polyisoprenylated in Arabidopsis thaliana.
Isoprenoid lipids were found to be covalently linked to proteins of Arabidopsis thaliana. Their identity (polyprenols: Prenol-9-11 with Pren-10 dominating and dolichols: Dol-15-17 with Dol-16 dominating) was confirmed by means of HPLC/ESI-MS with application of the multiple reaction monitoring technique as well as metabolic labeling of Arabidopsis plants with [(3)H]mevalonate and other precursors. The occurrence of typical farnesol-, geranylgeraniol-, and phytol-modified proteins was also noted. Radioisotopic labeling allowed detection of several proteins that were covalently bound to mevalonate-derived isoprenoid alcohols. A significant portion of polyisoprenylated proteins was recovered in the cytosolic/light vesicular fraction of Arabidopsis cells upon subfractionation. Taken together our data prove that a subset of plant proteins is polyisoprenylated.
Gutkowska
Malgorzata
M
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warsaw, Poland.
Bieńkowski
Tomasz
T
Hung
Vo Si
VS
Wanke
Malgorzata
M
Hertel
Jozefina
J
Danikiewicz
Witold
W
Swiezewska
Ewa
E
D017360:Arabidopsis / Q000378:metabolism*; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D050356:Lipid Metabolism; D011485:Protein Binding; D017368:Protein Prenylation; D021241:Spectrometry, Mass, Electrospray Ionization; D013729:Terpenes / Q000302:isolation & purification / Q000378:metabolism
D029681:Arabidopsis Proteins; D013729:Terpenes