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Dynamics of the mobile insert helix in the domain III-IV of Aux/IAA17 probed by site-directed spin labeling and paramagnetic NMR spectroscopy

  • Han, Mookyoung (Department of Agricultural Biotechnology, Seoul National University) ;
  • Suh, Jeong-Yong (Department of Agricultural Biotechnology, Seoul National University)
  • Received : 2015.08.02
  • Accepted : 2015.09.25
  • Published : 2015.10.10

Abstract

The plant hormone auxin is involved in all stages of plant development. Aux/IAAs are the transcriptional repressors that bind to the Auxin Response Factors (ARFs) to regulate the gene expression upon auxin release. Aux/IAA have highly conserved C-terminal domains (domains III-IV) that mediate both homotypic and heterotypic interactions between Aux/IAA and ARF family proteins. Recent studies revealed that the conserved domains III-IV share a common ${\beta}$-grasp fold that oligomerizes in a front-to-back manner. In particular, Aux/IAA contains a mobile insert helix in the domain III-IV, whereas ARFs do not. Here, we investigated the dynamics of the insert helix using paramagnetic NMR spectroscopy. The insert helix exhibited fast motions in the ps-ns time scale from $^{15}N$ relaxation data, but the amplitude of the motion is likely limited to the local neighborhood. Our result suggests that the motion of the helix may have functional implications in protein-protein interactions for transcriptional regulations.

Keywords

References

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