ArticleMicrobial biotechnology2011
Forkhead-associated proteins genetically linked to the serine/threonine kinase PknB regulate carbon flux towards antibiotic biosynthesis in Streptomyces coelicolor.
Article in Microbial biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Roles of PknB and CslA in Cell Wall Morphogenesis of Streptomyces.Molecular microbiology · 2026Article
- Enhancement of acyl-CoA precursor supply for increased avermectin B1a production by engineering meilingmycin polyketide synthase and key primary metabolic pathway genes.Microbial biotechnology · 2024Article
- OrthoRefine: automated enhancement of prior ortholog identification via synteny.BMC bioinformatics · 2024Article
- Distribution of PASTA domains in penicillin-binding proteins and serine/threonine kinases of Actinobacteria.The Journal of antibiotics · 2016Review
- Self-resistance in Streptomyces, with Special Reference to β-Lactam Antibiotics.Molecules (Basel, Switzerland) · 2016Review
- The external PASTA domain of the essential serine/threonine protein kinase PknB regulates mycobacterial growth.Open biology · 2015Article
- Cytoskeletal proteins of actinobacteria.International journal of cell biology · 2012Article
- Directed evolution, natural products for cancer chemotherapy, and micro-biosensing robots.Microbial biotechnology · 2011Article
- Streptomycetes.Microbial biotechnology · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
To date, the function of only two of the 34 predicted serine/threonine protein kinases (STPKs) of Streptomyces coelicolor has been described. Here we report functional analysis of pknB and two linked genes, fhaAB, encoding forkhead-associated (FHA) domain proteins that are part of a highly conserved gene locus in actinobacteria. In contrast to the homologous gene of Mycobacterium tuberculosis, pknB in S. coelicolor is not essential and has no apparent role in defining cell shape. Phosphorylation of recombinant forms of both the full-length protein and N-terminal kinase domain suggest that PknB-mediated signalling in S. coelicolor may be modulated by another factor(s). FhaAB are candidate interacting partners of PknB and loss of their function resulted in deregulation of central carbon metabolism, with carbon flux diverted to synthesis of the antibiotic actinorhodin. The substrate hyphae of the fhaAB mutant also exhibited an unusual cording morphology. The results indicate that inactivation of FHA 'brake' proteins can potentially amplify the function of STPKs and, in this case, provide a means to overproduce antibiotics.
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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.