CVB3 3C binding studies

Copyright information:

Taken from "A novel cGUUAg tetraloop structure with a conserved yYNMGg-type backbone conformation from cloverleaf 1 of bovine enterovirus 1 RNA"

Nucleic Acids Research 2005;33(6):2003-2011.

Published online 6 Apr 2005

PMCID:PMC1074726.

© The Author 2005. Published by Oxford University Press. All rights reserved

() Binding of CVB3 3C and 3CD to the SLD of cloverleaf 1 and cloverleaf 2, respectively, of BEV1 as assayed in yeast three-hybrid experiments. Wild-type SLD of cloverleaf 1 (BEV1-CL1-SLD), mutant of BEVSLD, from which G62 and U63 were deleted (BEV1-CL1-SLD-ΔG62U63) and wild-type SLD of cloverleaf 2 (BEV1-CL2-SLD). The rabbit iron-regulatory protein 1 (IRP) and the rat ferritin light chain iron-responsive element (IRE) were used as control. () Superimposition of (H,C)-HSQC spectra for the aromatic regions (H2C2, H6C6 and H8C8) of BEVSLD acquired in the presence (grey contours) and absence of 3C (thick black contours). Residues indicated by nucleotide type and residue number are discussed in the text. Asterisks denote new resonances appearing in the complex. () The residues most affected in the complex are indicated on the secondary structure of BEVSLD using grey boxes (see text for discussion). () Binding of CVB3 3C to wild-type and mutant BEVSLD RNAs as analysed by using EMSA. RNA was detected by ethidium bromide staining. The concentration of 3C and of the respective RNA present in the binding reaction before gel electrophoresis is indicated. Wild-type SLD of cloverleaf 1 (BEVSLD), mutant of BEVSLD (BEVSLD U64A), where U64 was replaced by an A.