Atomic structure of the regulatory TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA

FEBS Letters

article

Joon Shin¹  Bharti Singal¹  Ardina Grüber¹  David Meng Kit Wong¹  Priya Ragunathan¹  Gerhard Grüber¹ 

[1] School of Biological Sciences, Nanyang Technological University

关键词: Mycobacterium tuberculosis;    NMR spectroscopy;    Rel;    stringent response;    TGS domain;    tuberculosis;   

DOI  :  10.1002/1873-3468.14236

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 ( Mt Rel TGS), consisting of five antiparallel β-strands and one helix–loop–helix motif. The interaction of Mt Rel TGS with deacylated tRNA is shown, indicating the critical amino acids of Mt Rel TGS in tRNA binding, and presenting the first structural evidence of Mt Rel TGS binding to deacylated tRNA in solution in the absence of the translational machinery.

【 授权许可】

Unknown