Isopentenoid synthesis in embryonic Drosophila cells: prenylated protein profile and prenyl group usage.
Isopentenoid synthesis in embryonic Drosophila cells: prenylated protein profile and prenyl group usage.
复制标题
胚胎果蝇细胞中的类戊烯合成：异戊二烯化蛋白质谱和异戊二烯基团的使用。
DOI：
10.1016/0003-9861(92)90535-5
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发表时间：
1992
影响因子：
3.9
通讯作者：
Watson,JA
中科院分区：
文献类型：
--
作者：
Havel,CM;Fisher,P;Watson,JA
It has been established that vertebrates and yeasts modified a unique subset of polypeptides with farnesyl and geranylgeranyl residues. This observation has been extended toDrosophilaKccells. [3H]Mevalonate was incorporated into 54 Kccell peptides (18–92 kDa). As reported for mammalian cells, most of the labeled peptides had molecular weights between 21 and 27 kDa. C18radio-HPLC tryptic digest profiles for delipidized, [3H]mevalonate-labeled (a) insect (DrosophilaandSpodoptera frugiperda) and mammalian (Chinese hamster ovary met 18-2b) cells, (b) Kccell nuclear lamin, and (c) a 23.5-kDa purified Kccell GTP-binding protein were compared and analyzed. [35S]Cysteine-labeled Kccells yielded a tryptic digest radio-HPLC profile which was congruent with that for [3H]mevalonate-labeled cells. A significant fraction (30–33%) of the doubly labeled tryptic peptides were eluted with ⩾93% acetonitrile. Kccell nuclear lamin tryptic digests yielded a single3H-labeled product which migrated asS-farnesylcysteine. The Kccell 23.5-kDa GTP-binding protein's3H-labeled oligopeptide(s)/amino acid(s) was geranylgeranylated and its tryptic digest profile was representative of prenylated proteins whose oligopeptides eluted with ⩾93% acetonitrile. Moreover, the3H-labeled oligopeptide/amino acid profiles plus prenyl group patterns for [3H]mevalonate-labeled Kcand mammalian cell total extracts were similar. Collectively, these observations supported a prenylated protein spectrum and prenyl group usage as highly conserved eukaryotic cellular characteristics.
