ArticleJournal of bacteriology2008
The growth-promoting and stress response activities of the Bacillus subtilis GTP binding protein Obg are separable by mutation.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 29 citations in OpenAlex.
- Ectopic overexpression and CRISPRi-based knockdown ofJournal of bacteriology · 2025Article
- The Universally Conserved ATPase YchF Regulates Translation of Leaderless mRNA in Response to Stress Conditions.Frontiers in molecular biosciences · 2021Article
- The Stress-Responsive Alternative Sigma Factor SigB ofFrontiers in microbiology · 2020Review
- RiceG3 (Bethesda, Md.) · 2018Article
- Complementation of the Mycoplasma synoviae MS-H vaccine strain with wild-type obg influencing its growth characteristics.PloS one · 2018Article
- The bacterial translation stress response.FEMS microbiology reviews · 2014Review
- Structural and functional insights into the mode of action of a universally conserved Obg GTPase.PLoS biology · 2014Article
- Simulations of stressosome activation emphasize allosteric interactions between RsbR and RsbT.BMC systems biology · 2013Article
- The universally conserved prokaryotic GTPases.Microbiology and molecular biology reviews : MMBR · 2011Review
- Solution structure of the guanine nucleotide-binding STAS domain of SLC26-related SulP protein Rv1739c from Mycobacterium tuberculosis.The Journal of biological chemistry · 2011Article
- STAS domain structure and function.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2011Review
- Molecular modeling study for interaction between Bacillus subtilis Obg and Nucleotides.PloS one · 2010Article
- The ObgE/CgtA GTPase influences the stringent response to amino acid starvation in Escherichia coli.Molecular microbiology · 2009Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Bacillus subtilis Obg is a ribosome-associating GTP binding protein that is needed for growth, sporulation, and induction of the bacterium's general stress regulon (GSR). It is unclear whether the roles of Obg in sporulation and stress responsiveness are direct or a secondary effect of its growth-promoting functions. The present work addresses this question by an analysis of two obg alleles whose phenotypes argue for direct roles for Obg in each process. The first allele [obg(G92D)] encodes a missense change in the protein's highly conserved "obg fold" region. This mutation impairs cell growth and the ability of Obg to associate with ribosomes but fails to block sporulation or the induction of the GSR. The second obg mutation [obg(Delta22)] replaces the 22-amino-acid carboxy-terminal sequence of Obg with an alternative 26-amino-acid sequence. This Obg variant cofractionates with ribosomes and allows normal growth but blocks sporulation and impairs the induction of the GSR. Additional experiments revealed that the block on sporulation occurs early, preventing the activation of the essential sporulation transcription factor Spo0A, while inhibition of the GSR appears to involve a failure of the protein cascade that normally activates the GSR to effectively catalyze the reactions needed to activate the GSR transcription factor (sigma(B)).
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