秀丽隐杆线虫多肽的异戊二烯化

Robert A. Aspbury, Mark C. Prescott, Michael J. Fisher, Huw H. Rees
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引用次数: 6

摘要

真核生物蛋白的共价修饰,包括添加异戊二烯基团,是一种普遍的现象。在这里,我们提供了这种形式的共价修饰在自由生活的线虫,秀丽隐杆线虫的直接证据。在[3H]mevalonolactone存在下孵育后,特定的秀丽隐杆线虫多肽在水溶液和富含洗涤剂(Triton X-114)的提取物中被标记。从秀丽隐杆线虫多肽中剪切的修饰基团的化学和GC-MS分析显示,发生了香叶酰化,在较小程度上发生了靶多肽的法尼化。免疫印迹分析提供了初步证据,表明ras样let-60多肽是秀丽隐杆线虫异戊二烯化的靶点。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Isoprenylation of polypeptides in the nematode Caenorhabditis elegans

Covalent modification of eucaryotic proteins, involving addition of isoprenyl groups, is a widespread phenomenon. Here we provide direct evidence for this form of covalent modification in the free-living nematode, Caenorhabditis elegans. Following incubation in the presence of [3H]mevalonolactone, specific C. elegans polypeptides became labelled in both aqueous and detergent (Triton X-114)-enriched extracts. Chemical and GC–MS analysis of modifying groups, cleaved from C. elegans polypeptides, revealed that geranylgeranylation and, to a lesser extent, farnesylation of target polypeptides occurred. Immunoblot analysis provided preliminary evidence that the ras-like let-60 polypeptide was a target for isoprenylation in C. elegans.

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