Proteins are polyisoprenylated in Arabidopsis thaliana

被引:22
作者
Gutkowska, M
Bienkowski, T
Hung, VS
Wanke, M
Hertel, J
Danikiewicz, W
Swiezewska, E
机构
[1] Polish Acad Sci, Inst Biochem & Biophys, PL-02106 Warsaw, Poland
[2] Polish Acad Sci, Inst Organ Chem, PL-01224 Warsaw, Poland
关键词
protein prenylation; dolichol; electrospray ionization mass spectrometry; Arabidopsis thaliana;
D O I
10.1016/j.bbrc.2004.08.025
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 [H-3]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. (C) 2004 Published by Elsevier Inc.
引用
收藏
页码:998 / 1004
页数:7
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