Levicán Gloria, Katz Assaf, Valenzuela Patricio, Söll Dieter, Orellana Omar
Programa de Biologia Celular y Molecular, Instituto de Ciencias Biomédicas, Facultad de Medicina, Universidad de Chile, Casilla 70086, Santiago 838-0453, Chile.
FEBS Lett. 2005 Nov 21;579(28):6383-7. doi: 10.1016/j.febslet.2005.09.100. Epub 2005 Oct 25.
Glu-tRNA is either bound to elongation factor Tu to enter protein synthesis or is reduced by glutamyl-tRNA reductase (GluTR) in the first step of tetrapyrrole biosynthesis in most bacteria, archaea and in chloroplasts. Acidithiobacillus ferrooxidans, a bacterium that synthesizes a vast amount of heme, contains three genes encoding tRNA(Glu). All tRNA(Glu) species are substrates in vitro of GluRS1 from A. ferrooxidans.Glu-tRNA(3)(Glu), that fulfills the requirements for protein synthesis, is not substrate of GluTR. Therefore, aminoacylation of tRNA(3)(Glu) might contribute to ensure protein synthesis upon high heme demand by an uncoupling of protein and heme biosynthesis.
在大多数细菌、古细菌和叶绿体中,谷氨酰胺-tRNA(Glu-tRNA)要么与延伸因子Tu结合以进入蛋白质合成过程,要么在四吡咯生物合成的第一步被谷氨酰胺-tRNA还原酶(GluTR)还原。嗜酸氧化亚铁硫杆菌是一种能合成大量血红素的细菌,它含有三个编码tRNA(Glu)的基因。所有tRNA(Glu)种类在体外都是嗜酸氧化亚铁硫杆菌GluRS1的底物。满足蛋白质合成要求的Glu-tRNA(3)(Glu)不是GluTR的底物。因此,tRNA(3)(Glu)的氨酰化作用可能通过蛋白质和血红素生物合成的解偶联作用,在血红素需求较高时有助于确保蛋白质合成。