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Functional evidence for D‐ and T‐loop interactions in tmRNA
Author(s) -
Barends Sharief,
Björk Karl,
Gultyaev Alexander P.,
de Smit Maarten H.,
Pleij Cornelis W.A.,
Kraal Barend
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02306-2
Subject(s) - ef tu , transfer rna , ribosome , biology , elongation factor , phylogenetic tree , stem loop , genetics , protein tertiary structure , translation (biology) , rna , computational biology , chemistry , messenger rna , biochemistry , gene
During bacterial protein synthesis, stalled ribosomes can be rescued by tmRNA, a molecule with both tRNA and mRNA features. The tRNA region of tmRNA has sequence similarity with tRNA Ala and also has a clover‐leaf structure folded similarly as in canonical tRNAs. Here we propose the L‐shape of tmRNA to be stabilized by two tertiary interactions between its D‐ and T‐loop on the basis of phylogenetic and experimental evidence. Mutational analysis clearly demonstrates a tertiary interaction between G 13 and U 342 . Strikingly, this in evolution conserved interaction is not primarily important for tmRNA alanylation and for binding to elongation factor Tu, but especially for a proper functioning of SmpB.