Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA
| Autor: | Priya Ragunathan, Gerhard Grüber, David Meng Kit Wong, Bharti Singal, Ardina Grüber, Shin Joon |
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| Přispěvatelé: | School of Biological Sciences |
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Stringent response Biophysics GTPase Antiparallel (biochemistry) NMR Spectroscopy Biochemistry Bacterial Proteins Protein Domains RNA Transfer Structural Biology Hydrolase Genetics Amino Acid Sequence Cloning Molecular Molecular Biology chemistry.chemical_classification Chemistry Biological sciences [Science] nutritional and metabolic diseases Acetylation Mycobacterium tuberculosis Cell Biology GTP Pyrophosphokinase TRNA binding Amino acid Transfer RNA lipids (amino acids peptides and proteins) Mycobacterium Tuberculosis Protein Binding |
| Zdroj: | FEBS Letters. 595:3006-3018 |
| ISSN: | 1873-3468 0014-5793 |
| DOI: | 10.1002/1873-3468.14236 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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