Cited by 77Bacterial Genetics and BiotechnologyBiochemical and Molecular ResearchMicrobial Metabolic Engineering and Bioproduction

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The ObgE/CgtA GTPase influences the stringent response to amino acid starvation in Escherichia coli

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Persky, Nicole S., Ferullo, Daniel J., Cooper, Deani L., Moore, Hayley R., Lovett, Susan T.·2009·Molecular Microbiology

DOI 10.1111/j.1365-2958.2009.06767.xPMC PMC2771346

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Abstract

Summary: The stringent response is important for bacterial survival under stressful conditions, such as amino acid starvation, and is characterized by the accumulation of ppGpp and pppGpp. ObgE (CgtA, YhbZ) is an essential conserved GTPase in Escherichia coli and several observations have implicated the protein in the control of the stringent response. However, consequences of the protein on specific responses to amino acid starvation have not been noted. We show that ObgE binds to ppGpp with biologically relevant affinity in vitro, implicating ppGpp as an in vivo ligand of ObgE. ObgE mutants increase the ratio of pppGpp to ppGpp within the cell during the stringent response. These changes are correlated with a delayed inhibition of DNA replication by the stringent response, delayed resumption of DNA replication after release, as well as a decreased survival after amino acid deprivation. With these data, we place ObgE as an active effector of the response to amino acid starvation in vivo. Our data correlate the pppGpp/ppGpp ratio with DNA replication control under bacterial starvation conditions, suggesting a possible role for the relative balance of these two nucleotides.

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Bradford, M. M. (1976) · Analytical Biochemistry · doi:10.1016/0003-2697(76)90527-3 · Cited by 255,302
Escherichia coli and Salmonella :cellular and molecular biology
Neidhardt, F. C. (1996) · ASM Press eBooks · Cited by 8,197
The Complete Genome Sequence of Escherichia coli K-12
Blattner, F. R., Plunkett, G., Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado‐Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., et al. (1997) · Science · doi:10.1126/science.277.5331.1453 · Cited by 7,609
High efficiency transformation of E.coli by high voltage electroporation
Dower, W. J., Miller, J. F., & Ragsdale, C. W. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.13.6127 · Cited by 2,821
(p)ppGpp: Still Magical?
Potrykus, K., & Cashel, M. (2008) · Annual Review of Microbiology · doi:10.1146/annurev.micro.62.081307.162903 · Cited by 1,170
The stringent response
Cashel, M. (1996) · Medical Entomology and Zoology · Cited by 860
The OxyS regulatory RNA represses rpoS translation and binds the Hfq (HF‐I) protein
Zhang, A., Altuvia, S., Tiwari, A., Argaman, L., Hengge‐Aronis, R., & Storz, G. (1998) · The EMBO Journal · doi:10.1093/emboj/17.20.6061 · Cited by 785
A collection of strains containing genetically linked alternating antibiotic resistance elements for genetic mapping of Escherichia coli
Singer, M., Baker, T. A., Schnitzler, G. R., Deischel, S. M., Goel, M. C., Dove, W. F., Siranosian, K. J., Grossman, A. D., Erickson, J. W., & Gross, C. A. (1989) · Microbiological Reviews · doi:10.1128/mr.53.1.1-24.1989 · Cited by 738
Residual guanosine 3‘,5‘-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations.
Xiao, H., Kálmán, M., Ikehara, K., Zemel, S., Glaser, G., & Cashel, M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)67694-5 · Cited by 721
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Traxler, M. F., Summers, S. M., Nguyen, H., Zacharia, V. M., Hightower, G. A., Smith, J. T., & Conway, T. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06229.x · Cited by 519

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References
(2020) · Wiley eBooks · doi:10.1002/9781119309697.ref
Cellular and molecular outcomes of Pseudomonas putida KT2440 exposure to aluminium
Abdeljelil, N., Yahia, N. B. M., Landoulsi, A., Chatti, A., Wattiez, R., Houdt, R. V., & Gillan, D. C. (2025) · Folia Microbiologica · doi:10.1007/s12223-025-01380-3
Identification of factors regulating guanosine tetraphosphate (ppGpp) biosynthesis in Arabidopsis thaliana
Ke, H. (2016) · theses.fr (ABES) · doi:10.70675/d9cf34d4z992az41ecz86a6z2609af07dde2
Identification et caractérisation de nouvelles protéines impliquées dans la régulation des activités de l'alarmone synthétase SpoT chez Escherichia coli
Guiraud, P. (2021) · theses.fr (ABES) · doi:10.70675/314784b2zecf0z429dzb596ze0b56fd2c175
Epistatic interaction between ribosome-associated Era GTPase and stringent response regulator RelA modulates bacterial cell growth and dormancyPreprint
Pal, R., Sharma, H., Sabharwal, P., Vinothkumar, K. R., & Anand, B. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.21.719802

Authors: Persky, N. S., Ferullo, D. J., Cooper, D. L., Moore, H. R., & Lovett, S. T.
Affiliations: Brandeis University (US)
Corresponding author: Lovett, Susan T.
ORCID: Persky, Nicole S.
Lovett, Susan T.
Venue: Molecular Microbiology
Publisher: Wiley
Published: 2009-07
Volume: 73
Issue: 2
Pages: 253-266
ISSN: 0950-382X (ISSN-L)
1365-2958
DOI: 10.1111/j.1365-2958.2009.06767.x
PMC: PMC2771346
OpenAlex: W2162380932
Cited by: 77
References: 55
Citations by year: 2026: 2 · 2025: 2 · 2024: 7 · 2023: 1 · 2022: 3 · 2021: 6 · 2020: 6 · 2019: 6 · 2018: 5 · 2017: 3 · 2016: 8 · 2015: 5 · 2014: 6 · 2013: 5 · 2012: 4
FWCI: 2.33
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Molecular Microbiology (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health
U.S. Public Health Service (R01 G51753, R01 G79510, T32 G07596)
National Institute of General Medical Sciences (T32GM007596, R01GM079510, R01GM051753)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
Keywords: stringent response, GTPase, ppGpp, pppGpp, amino acid starvation, DNA replication inhibition, Escherichia coli, starvation survival
MeSH terms: Amino Acids, DNA Replication, DNA, Bacterial, Escherichia coli, Guanosine Tetraphosphate, Serine, Monomeric GTP-Binding Proteins, Escherichia coli Proteins

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The ObgE/CgtA GTPase influences the stringent response to amino acid starvation in Escherichia coli

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