The Helicobacter pylori Amidotransferase GatCAB Is Equally Efficient in Glutamine-dependent Transamidation of Asp-tRNAAsn and Glu-tRNAGln
نویسندگان
چکیده
منابع مشابه
Gln-tRNAGln synthesis in a dynamic transamidosome from Helicobacter pylori, where GluRS2 hydrolyzes excess Glu-tRNAGln
In many bacteria and archaea, an ancestral pathway is used where asparagine and glutamine are formed from their acidic precursors while covalently linked to tRNA(Asn) and tRNA(Gln), respectively. Stable complexes formed by the enzymes of these indirect tRNA aminoacylation pathways are found in several thermophilic organisms, and are called transamidosomes. We describe here a transamidosome form...
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tRNA-dependent amidotransferases (AdT) are essential enzymes for protein biosynthesis in many bacteria and in all archaea. As AdT is essential for a number of pathogenic bacteria, and it is absent from mammalian cytoplasm, it is considered as a putative target for novel inhibitors that could be lead compounds to develop a new class of antibiotics. Besides GatFAB of Saccharomyces cerevisiae mito...
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Aminoacyl-tRNA synthetases play a central role in protein synthesis by covalently linking the correct amino acid to the correct tRNA (1). Each aminoacyl-tRNA is then carried to the ribosome where it interacts with the cognate trinucleotide codon on the mRNA and transfers the amino acid onto a growing polypeptide chain. Work on tRNAs and aminoacyltRNA synthetases from bacteria, fungi, plants, an...
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متن کاملA single tRNA base pair mediates bacterial tRNA-dependent biosynthesis of asparagine
In many prokaryotes and in organelles asparagine and glutamine are formed by a tRNA-dependent amidotransferase (AdT) that catalyzes amidation of aspartate and glutamate, respectively, mischarged on tRNAAsn and tRNAGln. These pathways supply the deficiency of the organism in asparaginyl- and glutaminyl-tRNA synthtetases and provide the translational machinery with Asn-tRNAAsn and Gln-tRNAGln. So...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2007
ISSN: 0021-9258
DOI: 10.1074/jbc.m700398200