Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
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High-pressure NMR analysis on Escherichia coli IscU

  • Jongbum Na (Department of New Biology, Daegu Gyeongbuk Institute of Science and Technology) ;
  • Jinbeom Si (Department of New Biology, Daegu Gyeongbuk Institute of Science and Technology) ;
  • Jin Hae Kim (Department of New Biology, Daegu Gyeongbuk Institute of Science and Technology)
  • Received : 2024.03.18
  • Accepted : 2024.03.19
  • Published : 2024.03.20
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Abstract

IscU, the iron-sulfur (Fe-S) cluster scaffold protein, is an essential protein for biogenesis of Fe-S clusters. Previous studies showed that IscU manifests a metamorphic structural feature; at least two structural states, namely the structured state (S-state) and the disordered state (D-state), interconverting in a physiological condition, was observed. Moreover, subsequent studies demonstrated that the metamorphic flexibility of IscU is important for its Fe-S cluster assembly activity as well as for an efficient interaction with various partner proteins. Although solution nuclear magnetic resonance (NMR) spectroscopy has been a useful tool to investigate this protein, the detailed molecular mechanism that sustains the structural heterogeneity of IscU is still unclear. To tackle this issue, we applied a high-pressure NMR (HP-NMR) technique to the IscU variant, IscU(I8K), which shows an increased population of the S-state. We found that the equilibrium between the S- and D-state was significantly perturbed by pressure application, and the specific regions of IscU exhibited more sensitivity to pressure than the other regions. Our results provide novel insights to appreciate the dynamic behaviors of IscU and the related versatile functionality.

Keywords

Acknowledgement

We are deeply indebted to Dr. Kyoung-Seok Ryu, Dr. Eun-Hee Kim, Dr. Hae-Kap Cheong, and Mr. Joonhyeok Choi (Korea Basic Science Institute, Republic of Korea) for their help to conduct the HP-NMR experiments. This research used the NMR spectrometer that are maintained by the Ochang center of Korea Basic Science Institute. This research was supported by the National Research Foundation of Korea (NRF) funded by the Ministry of Science & ICT (NRF-2020R1I1A2074335).

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