NMR evidence
for formation of the SLIsbΔIa/SLV complex. (A)
Proposed secondary structure of SLIsbΔIa, a shiftable SLI variant,
and SLV in their free (left) and bound (right) forms. The boxed nucleotides
in SLIsbΔIa are those involved in the helix shift associated
with SLV binding. (B) Imino region of 1D 1H NMR spectra
recorded for the titration of 15N-labeled SLV with unlabeled
SLIsbΔIa. 1D NMR spectra were collected under the same conditions
and plotted on the same vertical scale but were adjusted to take into
account sample dilution during the titration. Imino proton assignment
is provided for both SLIsbΔIa and SLV in their free forms. The
imino proton signals marked with an asterisk in the 1:1 SLIsbΔIa/SLV
complex represent a small excess of free SLV. (C) Imino region of
the 2D NOESY spectrum of the SLIsbΔIa/15N-SLV complex.
On top, 1D 15N-filtered (purple; SLIsbΔIa) and 15N-edited (green; SLV) spectra of the complex annotated with
imino proton assignments. Annotations in (B) and (C) are used to identify
imino signals within SLIsbΔIa (purple), within SLV (green),
and at the kissing-loop junction (orange), and these imino signals
provide evidence for the base pairs shaded with the corresponding
colors in (A).