ArticleProtein science : a publication of the Protein Society2006
Molecular dissection of the mycobacterial stringent response protein Rel.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers, 1 of them a synthesis that pooled it.
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43 citing papers in PubMed, 1 synthesis or guideline pooled it, 90 citations in OpenAlex.
- Identification of gene targets against dormant phase Mycobacterium tuberculosis infections.BMC infectious diseases · 2007Pooled it
- Structural and functional relevance of the DUF4352 domain in antiviral immunity and physiology of mycobacteria.Nucleic acids research · 2025Article
- The N-Terminal Extension of theAntibiotics (Basel, Switzerland) · 2025Article
- Mycobacterium smegmatis MfpC is a GEF that regulates mfpA translationally to alter the fluoroquinolone efficacy.Communications biology · 2024Article
- An intramolecular cross-talk in D29 mycobacteriophage endolysin governs the lytic cycle and phage-host population dynamics.Science advances · 2024Article
- Rel-dependent decrease in the expression of ribosomal protein genes by inhibition of the respiratory electron transport chain inFrontiers in microbiology · 2024Article
- Article
- Tale of Twin Bifunctional Second Messenger (p)ppGpp Synthetases and Their Function in Mycobacteria.ACS omega · 2023Review
- Starvation sensing by mycobacterial RelA/SpoT homologue through constitutive surveillance of translation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mycobacterial Regulatory Systems Involved in the Regulation of Gene Expression Under Respiration-Inhibitory Conditions.Journal of microbiology (Seoul, Korea) · 2023Review
- The structure of DarB in complex with RelScience advances · 2023Article
- Genome-Wide Investigation of Pasteurella multocida Identifies the Stringent Response as a Negative Regulator of Hyaluronic Acid Capsule Production.Microbiology spectrum · 2022Article
- Fusion of the N-terminal 119 amino acids of RelA with the CTD domain render growth inhibitory effects of the latter, (p)ppGpp-dependent.Molecular genetics and genomics : MGG · 2022Article
- InJournal of bacteriology · 2022Article
- Stringent Response in Mycobacteria: From Biology to Therapeutic Potential.Pathogens (Basel, Switzerland) · 2021Review
- Ribosome association primes the stringent factor Rel for tRNA-dependent locking in the A-site and activation of (p)ppGpp synthesis.Nucleic acids research · 2021Article
- RelZ-Mediated Stress Response inJournal of bacteriology · 2020Article
- Article
- Pleiotropic Effects of Bacterial Small Alarmone Synthetases: Underscoring the Dual-Domain Small Alarmone Synthetases inFrontiers in microbiology · 2020Review
- YtfK activates the stringent response by triggering the alarmone synthetase SpoT in Escherichia coli.Nature communications · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Latency in Mycobacterium tuberculosis poses a barrier in its complete eradication. Overexpression of certain genes is one of the factors that help these bacilli survive inside the host during latency. Among these genes, rel, which leads to the expression of Rel protein, plays an important role by synthesizing the signaling molecule ppGpp using GDP and ATP as substrates, thereby changing bacterial physiology. In Gram-negative bacteria, the protein is thought to be activated in vivo in the presence of ribosome by sensing uncharged tRNA. In the present report, we show that Rel protein from Mycobacterium smegmatis, which is highly homologous to M. tuberculosis Rel, is functional even in the absence of ribosome and uncharged tRNA. From the experiments presented here, it appears that the activity of Rel(Msm) is regulated by the domains present at the C terminus, as the deletion of these domains results in higher synthesis activity, with little change in hydrolysis of ppGpp. However, in the presence of tRNA, though the synthesis activity of the full-length protein increases to a certain extent, the hydrolysis activity undergoes drastic reduction. Full-length Rel undergoes multimerization involving interchain disulfide bonds. The synthesis of pppGpp by the full-length protein is enhanced in the reduced environment in vitro, whereas the hydrolysis activity does not change significantly. Mutations of cysteines to serines result in monomerization with a simultaneous increase in the synthesis activity. Finally, it has been possible to identify the unique cysteine, of six present in Rel, required for tRNA-mediated synthesis of ppGpp.
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