Domain-specific recruitment of amide amino acids for protein synthesis

Debra L. Tumbula, Hubert D. Becker, Wei-zhong Chang and Dieter Söll
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Debra L. Tumbula: Yale University
Hubert D. Becker: Yale University
Wei-zhong Chang: Yale University
Dieter Söll: Yale University

Nature, 2000, vol. 407, issue 6800, 106-110

Abstract: Abstract The formation of aminoacyl-transfer RNA is a crucial step in ensuring the accuracy of protein synthesis. Despite the central importance of this process in all living organisms, it remains unknown how archaea and some bacteria synthesize Asn-tRNA and Gln-tRNA. These amide aminoacyl-tRNAs can be formed by the direct acylation of tRNA, catalysed by asparaginyl-tRNA synthetase and glutaminyl-tRNA synthetase, respectively. A separate, indirect pathway involves the formation of mis-acylated Asp-tRNAAsn or Glu-tRNAGln, and the subsequent amidation of these amino acids while they are bound to tRNA, which is catalysed by amidotransferases1,2. Here we show that all archaea possess an archaea-specific heterodimeric amidotransferase (encoded by gatD and gatE) for Gln-tRNA formation. However, Asn-tRNA synthesis in archaea is divergent: some archaea use asparaginyl-tRNA synthetase, whereas others use a heterotrimeric amidotransferase (encoded by the gatA, gatB and gatC genes). Because bacteria primarily use transamidation3, and the eukaryal cytoplasm uses glutaminyl-tRNA synthetase, it appears that the three domains use different mechanisms for Gln-tRNA synthesis; as such, this is the only known step in protein synthesis where all three domains have diverged. Closer inspection of the two amidotransferases reveals that each of them recruited a metabolic enzyme to aid its function; this provides direct evidence for a relationship between amino-acid metabolism and protein biosynthesis.

Date: 2000
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DOI: 10.1038/35024120

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