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Nucleic Acids Research Advance Access originally published online on January 31, 2007
Nucleic Acids Research 2007 35(4):1270-1278; doi:10.1093/nar/gkl1151
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Nucleic Acids Research, 2007, Vol. 35, No. 4 1270-1278
© 2007 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

RNA

Recognition of pyrrolysine tRNA by the Desulfitobacterium hafniense pyrrolysyl-tRNA synthetase

Stephanie Herring1, Alexandre Ambrogelly1, Carla R. Polycarpo1 and Dieter Söll1,2,*

Departments of 1Molecular Biophysics and Biochemistry and 2Chemistry Yale University, New Haven, CT 06520-8114, USA

*To whom Correspondence should be addressed. Tel: +1 203 432 6200; Fax: +1 203 432 6202; Email: soll{at}trna.chem.yale.edu

Received November 27, 2006. Revised December 16, 2006. Accepted December 17, 2006.

Pyrrolysine (Pyl), the 22nd co-translationally inserted amino acid, is incorporated in response to a UAG amber stop codon. Pyrrolysyl-tRNA synthetase (PylRS) attaches Pyl to its cognate tRNA, the special amber suppressor tRNAPyl. The genes for tRNAPyl (pylT) and PylRS (pylS) are found in all members of the archaeal family Methanosarcinaceae, and in Desulfitobacterium hafniense. The activation and aminoacylation properties of D. hafniense PylRS and the nature of the tRNAPyl identity elements were determined by measuring the ability of 24 mutant tRNAPyl species to be aminoacylated with the pyrrolysine analog N-{varepsilon}-cyclopentyloxycarbonyl-L-lysine. The discriminator base G73 and the first base pair (G1·C72) in the acceptor stem were found to be major identity elements. Footprinting analysis showed that PylRS binds tRNAPyl predominantly along the phosphate backbone of the T-loop, the D-stem and the acceptor stem. Significant contacts with the anticodon arm were not observed. The tRNAPyl structure contains the highly conserved T-loop contact U54·A58 and position 57 is conserved as a purine, but the canonical T- to D-loop contact between positions 18 and 56 was not present. Unlike most tRNAs, the tRNAPyl anticodon was shown not to be important for recognition by bacterial PylRS.

Present address: Carla R. Polycarpo, Instituto de Bioquimica Medica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brasil.


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