Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA
The stringent response is critical for the survival of Mycobacterium tuberculosis (Mtb) under nutrient starvation. The mechanism is mediated by a GTP pyrophosphokinase known as Rel, containing N-terminal synthetase and hydrolase domains and C-terminal regulatory domains, which include the TGS domain...
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sg-ntu-dr.10356-1617622022-09-19T06:31:50Z Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA Shin, Joon Singal, Bharti Grüber, Ardina Wong, David Meng Kit Ragunathan, Priya Grüber, Gerhard School of Biological Sciences Science::Biological sciences Mycobacterium Tuberculosis NMR Spectroscopy The stringent response is critical for the survival of Mycobacterium tuberculosis (Mtb) under nutrient starvation. The mechanism is mediated by a GTP pyrophosphokinase known as Rel, containing N-terminal synthetase and hydrolase domains and C-terminal regulatory domains, which include the TGS domain (ThrRS, GTPase, and SpoT proteins) that has been proposed to activate the synthetase domain via interaction with deacylated tRNA. Here, we present the NMR solution structure of the Mtb Rel TGS domain (MtRel TGS), consisting of five antiparallel β-strands and one helix-loop-helix motif. The interaction of MtRel TGS with deacylated tRNA is shown, indicating the critical amino acids of MtRel TGS in tRNA binding, and presenting the first structural evidence of MtRel TGS binding to deacylated tRNA in solution in the absence of the translational machinery. Ministry of Education (MOE) We would like to thank the Singapore Ministry of Education Academic Research Fund Tier 1 (Rg137/15)for the funding to GG. 2022-09-19T06:31:50Z 2022-09-19T06:31:50Z 2021 Journal Article Shin, J., Singal, B., Grüber, A., Wong, D. M. K., Ragunathan, P. & Grüber, G. (2021). Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA. FEBS Letters, 595(24), 3006-3018. https://dx.doi.org/10.1002/1873-3468.14236 0014-5793 https://hdl.handle.net/10356/161762 10.1002/1873-3468.14236 34808002 2-s2.0-85119970605 24 595 3006 3018 en Rg137/15 FEBS Letters © 2021 Federation of European Biochemical Societies. All rights reserved. |
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Science::Biological sciences Mycobacterium Tuberculosis NMR Spectroscopy Shin, Joon Singal, Bharti Grüber, Ardina Wong, David Meng Kit Ragunathan, Priya Grüber, Gerhard Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA |
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The stringent response is critical for the survival of Mycobacterium tuberculosis (Mtb) under nutrient starvation. The mechanism is mediated by a GTP pyrophosphokinase known as Rel, containing N-terminal synthetase and hydrolase domains and C-terminal regulatory domains, which include the TGS domain (ThrRS, GTPase, and SpoT proteins) that has been proposed to activate the synthetase domain via interaction with deacylated tRNA. Here, we present the NMR solution structure of the Mtb Rel TGS domain (MtRel TGS), consisting of five antiparallel β-strands and one helix-loop-helix motif. The interaction of MtRel TGS with deacylated tRNA is shown, indicating the critical amino acids of MtRel TGS in tRNA binding, and presenting the first structural evidence of MtRel TGS binding to deacylated tRNA in solution in the absence of the translational machinery. |
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School of Biological Sciences |
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School of Biological Sciences Shin, Joon Singal, Bharti Grüber, Ardina Wong, David Meng Kit Ragunathan, Priya Grüber, Gerhard |
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Article |
author |
Shin, Joon Singal, Bharti Grüber, Ardina Wong, David Meng Kit Ragunathan, Priya Grüber, Gerhard |
author_sort |
Shin, Joon |
title |
Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA |
title_short |
Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA |
title_full |
Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA |
title_fullStr |
Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA |
title_full_unstemmed |
Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA |
title_sort |
atomic structure of the regulatory tgs domain of rel protein from mycobacterium tuberculosis and its interaction with deacylated trna |
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2022 |
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https://hdl.handle.net/10356/161762 |
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1745574629801459712 |