ArticleJournal of bacteriology2015
Resuscitation-promoting factors are cell wall-lytic enzymes with important roles in the germination and growth of Streptomyces coelicolor.
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 26 papers.
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Who cites it
26 citing papers in PubMed, 40 citations in OpenAlex.
- Excavation of resources ofFrontiers in microbiology · 2025Article
- The DeoR-like pleiotropic regulator SCO1897 controls specialised metabolism, sporulation, spore germination, and phosphorus accumulation in Streptomyces coelicolor.Communications biology · 2024Article
- Functional connexion of bacterioferritin in antibiotic production and morphological differentiation in Streptomyces coelicolor.Microbial cell factories · 2024Article
- Resuscitation Promotion Factor: A Pronounced Bacterial Cytokine in Propelling Bacterial Resuscitation.Microorganisms · 2024Review
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- Role of Resuscitation Promoting Factor-like Protein fromMicroorganisms · 2023Article
- The resuscitation-promoting factor (Rpf) fromAccess microbiology · 2023Article
- Reaching unreachables: Obstacles and successes of microbial cultivation and their reasons.Frontiers in microbiology · 2023Review
- Metabolic engineering ofEngineering microbiology · 2022Review
- Enzymatic properties and biological activity of resuscitation-promoting factor B ofFrontiers in microbiology · 2022Article
- Structural, Metabolic and Evolutionary Comparison of Bacterial Endospore and Exospore Formation.Frontiers in microbiology · 2021Review
- Roles of LysM and LytM domains in resuscitation-promoting factor (Rpf) activity and Rpf-mediated peptidoglycan cleavage and dormant spore reactivation.The Journal of biological chemistry · 2020Article
- The feather degradation mechanisms of a new Streptomyces sp. isolate SCUT-3.Communications biology · 2020Article
- Alterations in the Cell Wall ofFrontiers in microbiology · 2020Article
- Cytosolic copper is a major modulator of germination, development and secondary metabolism in Streptomyces coelicolor.Scientific reports · 2019Article
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- Streptomyces Differentiation in Liquid Cultures as a Trigger of Secondary Metabolism.Antibiotics (Basel, Switzerland) · 2018Review
- Characterization of Sigma Factor Genes inFrontiers in microbiology · 2018Article
- Regulation of a muralytic enzyme-encoding gene by two non-coding RNAs.RNA biology · 2017Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Dormancy is a common strategy adopted by bacterial cells as a means of surviving adverse environmental conditions. For Streptomyces bacteria, this involves developing chains of dormant exospores that extend away from the colony surface. Both spore formation and subsequent spore germination are tightly controlled processes, and while significant progress has been made in understanding the underlying regulatory and enzymatic bases for these, there are still significant gaps in our understanding. One class of proteins with a potential role in spore-associated processes are the so-called resuscitation-promoting factors, or Rpfs, which in other actinobacteria are needed to restore active growth to dormant cell populations. The model species Streptomyces coelicolor encodes five Rpf proteins (RpfA to RfpE), and here we show that these proteins have overlapping functions during growth. Collectively, the S. coelicolor Rpfs promote spore germination and are critical for growth under nutrient-limiting conditions. Previous studies have revealed structural similarities between the Rpf domain and lysozyme, and our in vitro biochemical assays revealed various levels of peptidoglycan cleavage capabilities for each of these five Streptomyces enzymes. Peptidoglycan remodeling by enzymes such as these must be stringently governed so as to retain the structural integrity of the cell wall. Our results suggest that one of the Rpfs, RpfB, is subject to a unique mode of enzymatic autoregulation, mediated by a domain of previously unknown function (DUF348) located within the N terminus of the protein; removal of this domain led to significantly enhanced peptidoglycan cleavage.
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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.