Recognition of One tRNA by Two Classes of Aminoacyl-tRNA Synthetase View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1999

AUTHORS

M. Ibba , S. Bunjun , H. Losey , B. Min , D. Söll

ABSTRACT

Lysyl-tRNA synthetases are unique amongst the aminoacyl-tRNA synthetases in being composed of two unrelated families. In most bacteria and all eukarya, the known lysyl-tRNA synthetases are subclass He-type aminoacyl-tRNA synthetases whereas some archaea and bacteria have been shown to contain an unrelated class I-type lysyl-tRNA synthetase. We have now examined substrate recognition by a bacterial (from Borrelia burgdorferi) and an archaeal (from Methanococcus maripaludis) class I lysyl-tRNA synthetase. The genes encoding both enzymes were able to rescue an Escherichia coli strain deficient in lysyl-tRNA synthetase, indicating their ability to functionally substitute for class II lysyl-tRNA synthetases in vivo. In vitro characterization revealed lysine activation and recognition to be tRNA-dependent, a phenomenon previously reported for other class I aminoacyl-tRNA synthetases. More detailed examination of tRNA recognition has shown that class I lysyl-tRNA synthetases recognize the same elements in tRNALys as their class II counterparts; specifically, the discriminator base (N73) and the anticodon serve as recognition elements. The implications of these results for the evolution of Lys-tRNALys synthesis and their possible indications of a more ancient origin for tRNA then aminoacyl-tRNA synthetases will be discussed. More... »

PAGES

143-148

Book

TITLE

RNA Biochemistry and Biotechnology

ISBN

978-0-7923-5862-6
978-94-011-4485-8

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-94-011-4485-8_11

DOI

http://dx.doi.org/10.1007/978-94-011-4485-8_11

DIMENSIONS

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