Article thumbnail
Location of Repository

A tRNA(Glu) that uncouples protein and tetrapyrrole biosynthesis

By Gloria Levicán, Assaf Katz, Patricio Valenzuela, Dieter Söll and Omar Orellana

Abstract

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 tRNAG(3)(Glu) might contribute to ensure protein synthesis upon high heme demand by an uncoupling of protein and heme biosynthesis

Topics: EF-Tu, GluRS, GluTR, Heme, tRNA specificity
Publisher: 'Elsevier BV'
Year: 2005
DOI identifier: 10.1016/j.febslet.2005.09.100
OAI identifier: oai:repositorio.uchile.cl:2250/158898
Download PDF:
Sorry, we are unable to provide the full text but you may find it at the following location(s):
  • http://repositorio.uchile.cl/h... (external link)
  • Suggested articles


    To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.