Wang Yen-Chih, Distefano Mark D
Departments of Chemistry and Medicinal Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.
Departments of Chemistry and Medicinal Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.
Bioorg Chem. 2016 Feb;64:59-65. doi: 10.1016/j.bioorg.2015.12.003. Epub 2015 Dec 10.
Protein prenylation is a posttranslational modification catalyzed by prenyltransferases involving the attachment of farnesyl or geranylgeranyl groups to residues near the C-termini of proteins. This irreversible covalent modification is important for membrane localization and proper signal transduction. Here, the use of isoprenoid analogues for studying prenylated proteins is reviewed. First, experiments with analogues containing small fluorophores that are alternative substrates for prenyltransferases are described. Those analogues have been useful for quantifying binding affinity and for the production of fluorescently labeled proteins. Next, the use of analogues that incorporate biotin, bioorthogonal groups or antigenic moieties is described. Such probes have been particularly useful for identifying proteins that are naturally prenylated within mammalian cells. Overall, the use of isoprenoid analogues has contributed significantly to the understanding of protein prenlation.
蛋白质异戊二烯化是一种由异戊二烯基转移酶催化的翻译后修饰，涉及将法尼基或香叶基香叶基基团连接到蛋白质C末端附近的残基上。这种不可逆的共价修饰对于膜定位和适当的信号转导很重要。在此，综述了使用类异戊二烯类似物研究异戊二烯化蛋白质的情况。首先，描述了使用含有小荧光团的类似物进行实验，这些类似物是异戊二烯基转移酶的替代底物。这些类似物已用于定量结合亲和力和生产荧光标记的蛋白质。接下来，描述了使用掺入生物素、生物正交基团或抗原部分的类似物。此类探针对于鉴定哺乳动物细胞内天然异戊二烯化的蛋白质尤为有用。总体而言，类异戊二烯类似物的使用对理解蛋白质异戊二烯化有显著贡献。
