Ingoglia Nicholas A
New Jersey Medical School, Rutgers School of Biomedical Health Science, Newark, NJ, 07103, USA,
Methods Mol Biol. 2015;1337:25-32. doi: 10.1007/978-1-4939-2935-1_4.
Transfer RNA-mediated posttranslational protein modification by arginine has been demonstrated in vitro in axoplasm extruded from the giant axons of squid and in injured and regenerating vertebrate nerves. In nerve and axoplasm, the highest activity is found in a fraction of a 150,000 × g supernatant containing high molecular weight protein/RNA complexes but lacking molecules of <5 kDa. Arginylation (and protein modification by other amino acids) is not found in more purified, reconstituted fractions. The data are interpreted as indicating that it is critical to recover the reaction components in high molecular weight protein/RNA complexes in order to maintain maximum physiological activity. The level of arginylation is greatest in injured and growing vertebrate nerves compared with intact nerves, suggesting a role for these reactions in nerve injury/repair and during axonal growth.
在从鱿鱼巨轴突挤出的轴浆以及受损和再生的脊椎动物神经中,已在体外证明了转运RNA介导的精氨酸对蛋白质的翻译后修饰。在神经和轴浆中,最高活性存在于150,000×g上清液的一个组分中,该组分含有高分子量蛋白质/RNA复合物,但缺乏分子量小于5 kDa的分子。在更纯化的重组组分中未发现精氨酰化(以及其他氨基酸对蛋白质的修饰)。这些数据被解释为表明,为了维持最大的生理活性,回收高分子量蛋白质/RNA复合物中的反应成分至关重要。与完整神经相比,在受损和生长的脊椎动物神经中精氨酰化水平最高,这表明这些反应在神经损伤/修复以及轴突生长过程中发挥作用。