Structural basis for tRNA decoding and aminoacylation sensing by T-box riboregulators.

Publication Type:

Journal Article

Source:

Nat Struct Mol Biol, Volume 26, Issue 12, p.1106-1113 (2019)

Abstract:

<p>T-box riboregulators are a class of cis-regulatory RNAs that govern the bacterial response to amino acid starvation by binding, decoding and reading the aminoacylation status of specific transfer RNAs. Here we provide a high-resolution crystal structure of a full-length T-box from Mycobacterium tuberculosis that explains tRNA decoding and aminoacylation sensing by this riboregulator. Overall, the T-box consists of decoding and aminoacylation sensing modules bridged by a rigid pseudoknot structure formed by the mid-region domains. Stem-I and the Stem-II S-turn assemble a claw-like decoding module, while the antiterminator, Stem-III, and the adjacent linker form a tightly interwoven aminoacylation sensing module. The uncharged tRNA is selectively recognized by an unexpected set of favorable contacts from the linker region in the aminoacylation sensing module. A complex structure with a charged tRNA mimic shows that the extra moiety dislodges the linker, which is indicative of the possible chain of events that lead to alternative base-pairing and altered expression output.</p>

PDB: 
6UFG and 6UFH
Detector: 
PILATUS
Beamline: 
24-ID-C
Co-crystal structure of M. tuberculosis ileS T-box in complex with tRNA-3'-OH