Open AccessDomain–domain communication in a miniature archaebacterial tRNA synthetase
Author(s) -
Brian A. Steer,
Paul Schimmel
Publication year - 1999
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.96.24.13644
Subject(s) - transfer rna , aminoacyl trna synthetase , methanococcus , domain (mathematical analysis) , egf like domain , biology , amino acyl trna synthetases , amino acid , protein secondary structure , protein domain , computational biology , chemistry , biochemistry , rna , gene , archaea , mathematical analysis , mathematics
The three-dimensional structure of tRNA is organized into two domains-the acceptor-TPsiC minihelix with the amino acid attachment site and a second, anticodon-containing, stem-loop domain. Aminoacyl-tRNA synthetases have a structural organization that roughly recapitulates the two-domain organization of tRNAs-an older primary domain that contains the catalytic center and interacts with the minihelix and a secondary, more recent, domain that makes contacts with the anticodon-containing arm. The latter contacts typically are essential for enhancement of the catalytic constant k(cat) through domain-domain communication. Methanococcus jannaschii tyrosyl-tRNA synthetase is a miniature synthetase with a tiny secondary domain suggestive of an early synthetase evolving from a one-domain to a two-domain structure. Here we demonstrate functional interactions with the anticodon-containing arm of tRNA that involve the miniaturized secondary domain. These interactions appear not to include direct contacts with the anticodon triplet but nonetheless lead to domain-domain communication. Thus, interdomain communication may have been established early in the evolution from one-domain to two-domain structures.