DNA-rescuable allosteric inhibition of aptamer II ligand affinity by aptamer I element in the shortened Vibrio cholerae glycine riboswitch

    Authors

    E. M. Sherman; G. Elsayed; J. M. Esquiaqui; M. Elsayed; B. Brinda;J. D. Ye

    Comments

    Authors: contact us about adding a copy of your work at STARS@ucf.edu

    Abbreviated Journal Title

    J. Biochem.

    Keywords

    allosteric control; aptamer; cooperativity; genetic circuit; glycine; riboswitch; SYNTHETIC BIOLOGY; DEPENDENT RIBOSWITCH; RNA; BINDING; COOPERATIVITY; EXPRESSION; OLIGONUCLEOTIDE; RECOGNITION; MECHANISMS; MOTIFS; Biochemistry & Molecular Biology

    Abstract

    Glycine riboswitches contain two aptamers and turn on the expression of downstream genes in bacteria. Although full-length glycine riboswitches were shown to exhibit no glycine-binding cooperativity, the truncated glycine riboswitches were confirmed to bind two glycine molecules cooperatively. Thorough understanding of the ligand-binding cooperativity may shed light on the molecular basis of the cooperativity and help design novel intricate biosensing genetic circuits for application in synthetic biology. A previously proposed sequential model does not readily provide explanation for published data showing a deleterious mutation in the first aptamer inhibiting the glycine binding of the second one. Using the glycine riboswitch from Vibrio cholerae as a model system, we have identified a region in the first aptamer that modulates the second aptamer function especially in the shortened glycine riboswitch. Importantly, this modulation can be rescued by the addition of a complementary oligodeoxynucleotide, demonstrating the feasibility of developing this system into novel genetic circuits that sense both glycine and a DNA signal.

    Journal Title

    Journal of Biochemistry

    Volume

    156

    Issue/Number

    6

    Publication Date

    1-1-2014

    Document Type

    Article

    Language

    English

    First Page

    323

    Last Page

    331

    WOS Identifier

    WOS:000345770200004

    ISSN

    0021-924X

    Share

    COinS