Dynamics of the mobile insert helix in the domain III-IV of Aux/IAA17 probed by site-directed spin labeling and paramagnetic NMR spectroscopy
2
조회
0
다운로드
1
인용
0
참고문헌
키워드
초록
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 β-grasp fold that oligomerizes in a front-to-back manner.1,2,3 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 15N 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.
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 β-grasp fold that oligomerizes in a front-to-back manner.1,2,3 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 15N 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.
참고문헌 (7)
- M. Han, , Proc. Natl. Acad. Sci. USA, 111, pp.18613~ (2014)
- H. M, Nanao, , Nat. commun, 5 (2014)
- D. A. Korasick, , Proc. Natl. Acad. Sci. USA, 111, pp.5427~ (2014)
- D. C. Dinesh, , Proc. Natl. Acad. Sci. USA, 112, pp.6230~ (2015)
- T. Zheng, , Org. Biomol. Chem, 13, pp.1159~ (2015)
- 서정용, "NMR Studies on Transient Protein Complexes: Perspectives", Journal of the Korean Magnetic Resonance Society, 18(1), pp.1~4 (2014), 한국자기공명학회[DOI]
- 이인균, "Backbone 1H, 15N, and 13C Resonances Assignment and Secondary Structure Prediction of SAV0506 from Staphylococcus aureus", Journal of the Korean Magnetic Resonance Society, 17(1), pp.54~58 (2013), 한국자기공명학회[DOI]