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Author

Kim, Hajin
Single Molecule Biophysics Lab
Research Interests
  • Biophysics, Single Molecule, fluorescence Spectroscopy, biological Motors, biomolecular assembly

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Visualization of the nanospring dynamics of the I kappa B alpha ankyrin repeat domain in real time

Cited 17 times inthomson ciCited 15 times inthomson ci
Title
Visualization of the nanospring dynamics of the I kappa B alpha ankyrin repeat domain in real time
Author
Lamboy, Jorge A.Kim, HajinLee, Kyung SukHa, TaekjipKomives, Elizabeth A.
Keywords
Intrinsically disordered protein; NFkappaB; Protein dynamics; Transcription factor
Issue Date
201106
Publisher
NATL ACAD SCIENCES
Citation
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.108, no.25, pp.10178 - 10183
Abstract
IκBα is a crucial regulator of NFκB transcription. NFκB-mediated gene activation is robust because levels of free IκBα are kept extremely low by rapid, ubiquitin-independent degradation of newly synthesized IκBα. IκBα has a weakly folded ankyrin repeat 5-6 (AR5-6) region that is critical in establishing its short intracellular half-life. The AR5-6 region of IκBα folds upon binding to NFκB. The NFκB-bound IκBα has a long half-life and requires ubiquitin-targeted degradation. We present single molecule FRET evidence that the native state of IκBα transiently populates an intrinsically disordered state characterized by a more extended structure and fluctuations on the millisecond time scale. Binding to NFκB or introduction of stabilizing mutations in AR 6 suppressed the fluctuations, whereas higher temperature or small amounts of urea increased them. The results reveal that intrinsically disordered protein regions transition between collapsed and extended conformations under native conditions.
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DOI
http://dx.doi.org/10.1073/pnas.1102226108
ISSN
0027-8424
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