Modulation of quaternary structure and enhancement of ligand binding by the K-turn of tandem glycine riboswitches.

ABSTRACT: Most known glycine riboswitches have two homologous aptamer domains arranged in tandem and separated by a short linker. The two aptamers associate through reciprocal "quaternary" interactions that have been proposed to result in cooperative glycine binding. Recently, the interaptamer linker was found to form helix P0 with a previously unrecognized segment 5' to the first aptamer domain. P0 was shown to increase glycine affinity, abolish cooperativity, and conform to the K-turn motif consensus. We examine the global thermodynamic and structural role of P0 using isothermal titration calorimetry (ITC) and small-angle X-ray scattering (SAXS), respectively. To evaluate the generality of P0 function, we prepared glycine riboswitch constructs lacking and including P0 from Bacillus subtilis, Fusob

SUBMITTER: Baird NJ 

PROVIDER: S-EPMC3543082 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature