ArticleJournal of bacteriology2015
Proline metabolism increases katG expression and oxidative stress resistance in Escherichia coli.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 101 citations in OpenAlex.
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- Systems-level exploitation of OxyR regulon unravels a potential antibacterial target in Pseudomonas aeruginosa.Communications biology · 2025Article
- Proline dehydrogenase, a rate-limiting catabolic enzyme, affecting the growth and pathogenicity of Toxoplasma gondii tachyzoites by regulating the proline metabolism and mitochondrial function of the parasite.Parasites & vectors · 2025Article
- Protective Effects of Astaxanthin on Thioacetamide-Induced Hepatopancreatic Damage inAnimals : an open access journal from MDPI · 2025Article
- The Proline Dehydrogenase GeneInternational journal of molecular sciences · 2025Article
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- Synergistic effect of nitrate exposure and heatwaves on the growth, and metabolic activity of microalgae, Chlamydomonas reinhardtii, and Pseudokirchneriella subcapitata.Scientific reports · 2024Article
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- Chitosan nanoparticle encapsulation increased the prophylactic efficacy of Lactobacillus plantarum RM1 against AFMEnvironmental science and pollution research international · 2023Article
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- Critical Effect of HMicrobiology spectrum · 2022Article
- Metabolic Regulation Effect and Potential Metabolic Biomarkers of Pre-Treated Delphinidin on Oxidative Damage Induced by Paraquat in A549 Cells.Foods (Basel, Switzerland) · 2022Article
- Interplay between Proline Metabolism and ROS in the Fine Tuning of Root-Meristem Size inPlants (Basel, Switzerland) · 2022Article
- Proline confers acid stress tolerance to Bacillus megaterium G18.Scientific reports · 2022Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The oxidation of l-proline to glutamate in Gram-negative bacteria is catalyzed by the proline utilization A (PutA) flavoenzyme, which contains proline dehydrogenase (PRODH) and Δ(1)-pyrroline-5-carboxylate (P5C) dehydrogenase domains in a single polypeptide. Previous studies have suggested that aside from providing energy, proline metabolism influences oxidative stress resistance in different organisms. To explore this potential role and the mechanism, we characterized the oxidative stress resistance of wild-type and putA mutant strains of Escherichia coli. Initial stress assays revealed that the putA mutant strain was significantly more sensitive to oxidative stress than the parental wild-type strain. Expression of PutA in the putA mutant strain restored oxidative stress resistance, confirming that depletion of PutA was responsible for the oxidative stress phenotype. Treatment of wild-type cells with proline significantly increased hydroperoxidase I (encoded by katG) expression and activity. Furthermore, the ΔkatG strain failed to respond to proline, indicating a critical role for hydroperoxidase I in the mechanism of proline protection. The global regulator OxyR activates the expression of katG along with several other genes involved in oxidative stress defense. In addition to katG, proline increased the expression of grxA (glutaredoxin 1) and trxC (thioredoxin 2) of the OxyR regulon, implicating OxyR in proline protection. Proline oxidative metabolism was shown to generate hydrogen peroxide, indicating that proline increases oxidative stress tolerance in E. coli via a preadaptive effect involving endogenous hydrogen peroxide production and enhanced catalase-peroxidase activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.