Ellis J Chris, Barnes Jeffrey, Brown James W
Laboratory of Signal Transduction, NIEHS, Research Triangle Park, North Carolina, USA.
RNA Biol. 2007 Nov;4(3):169-72. doi: 10.4161/rna.4.3.5347.
It has been suggested that Alba, a well-established chromatin protein in Archaea, is also a subunit of the archaeal RNase P holoenzyme, based on the observation that the homolog of this protein in humans has been shown to be associated with RNase P activity. Using the same biochemical methods we used previously to show that four other proteins homologous to eukaryotic RNase P proteins are bona fide RNase P subunits in Archaea, we could not detect any association of the Alba homolog in Methanothermobacter thermoautotrophicus (Mth1483p) with the RNase P holoenzyme. In addition, the presence of Mth1483p did not enhance the activity of RNase P holoenzyme reconstituted from recombinant subunits. In conclusion, we find no evidence that Alba is an RNase P subunit.
有人提出，古菌中一种成熟的染色质蛋白阿尔巴（Alba）也是古菌核糖核酸酶P全酶的一个亚基，这是基于以下观察结果：该蛋白在人类中的同源物已被证明与核糖核酸酶P活性有关。我们之前使用相同的生化方法证明了与真核核糖核酸酶P蛋白同源的其他四种蛋白是古菌中真正的核糖核酸酶P亚基，但我们未能检测到嗜热自养甲烷杆菌（Methanothermobacter thermoautotrophicus，Mth1483p）中的阿尔巴同源物与核糖核酸酶P全酶有任何关联。此外，Mth1483p的存在并未增强由重组亚基重构的核糖核酸酶P全酶的活性。总之，我们没有发现证据表明阿尔巴是核糖核酸酶P的亚基。
