In Streptomyces lividans, the expression of several proteins is stimulated by the thiopeptide antibiotic thiostrepton. Two of these, TipAL and TipAS, autoregulate their expression after covalently binding to thiostrepton; this irreversibly sequesters the antibiotic and desensitizes the organism to its effects. In this work, additional molecular recognition interactions involved in this critical event were explored by utilizing various thiostrepton analogues and several site-directed mutants of the TipAS antibiotic binding protein. Dissociation constants for several thiostrepton analogues ranged from 0.19 to 12.95 μM, depending on the analogue. The contributions of specific structural elements of the thiostrepton molecule to this interaction have been discerned, and an unusual covalent modification between the antibiotic and a new residue in a TipAS mutant has been detected.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/cbic.201300724 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Mitigating genetic instability caused by the excision activity of the C31 integrase in .
Appl Environ Microbiol
December 2024
MOE Key Laboratory of Industrial Fermentation Microbiology, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.
Over the past three decades, the integrase (Int) from phage C31 has become a valuable genome engineering tool across various species. C31 Int was thought to mediate unidirectional site-specific integration ( × to and ) in the absence of the phage-encoded recombination directionality factor (RDF). However, we have shown in this study that Int can also catalyze reverse excision ( × to and ) at low frequencies in and , causing genetic instability in engineered strains.
View Article and Find Full Text PDFIdentification of plasmids from thermophilic Streptomyces strains and development of a gene cloning system for thermophilic Streptomyces species.
J Ind Microbiol Biotechnol
January 2024
Technology Research Association for Next-Generation Natural Products Chemistry, 2-4-7 Aomi, Koto-ku, Tokyo 135-0064, Japan.
Unlabelled: To develop a host-vector system for use in thermophilic Streptomyces, multi-copy plasmids were screened for thermophilic Streptomyces species using data from public bioresource centers (JCM and NBRC). Of 27 thermophilic Streptomyces strains, 3 harbored plasmids. One plasmid (pSTVU1), derived from S.
View Article and Find Full Text PDFRelationship between oriT length and efficiency of RP4-mediated conjugation from Escherichia coli to Gram-positive bacteria.
Biosci Biotechnol Biochem
December 2024
Department of Biomedical Engineering, Graduate School of Shinshu University, Nagano, Japan.
In RP4 conjugation, approximately 350 bp of the origin of transfer (oriT) is required for transfer. Within this oriT, there are binding regions for the transfer-related proteins TraI, TraK, and TraJ. We investigated the influence of deleting each protein-binding region within oriT on transfer efficiency in Escherichia coli, Streptomyces lividans, and Bacillus subtilis.
View Article and Find Full Text PDFThe acetyltransferase SCO0988 controls positively specialized metabolism and morphological differentiation in the model strains and .
Front Microbiol
July 2024
Department of Ecology, Institute of Hydrobiology, School of Life Science and Technology, Key Laboratory of Eutrophication and Red Tide Prevention of Guangdong Higher Education Institutes, Engineering Research Center of Tropical and Subtropical Aquatic Ecological Engineering, Ministry of Education, Jinan University, Guangzhou, China.
Streptomycetes are well-known antibiotic producers possessing in their genomes numerous silent biosynthetic pathways that might direct the biosynthesis of novel bio-active specialized metabolites. It is thus of great interest to find ways to enhance the expression of these pathways to discover most needed novel antibiotics. In this study, we demonstrated that the over-expression of acetyltransferase SCO0988 up-regulated the production of specialized metabolites and accelerated sporulation of the weak antibiotic producer, and that the deletion of this gene had opposite effects in the strong antibiotic producer, .
View Article and Find Full Text PDFElucidating the role of lipid interactions in stabilizing the membrane protein KcsA.
Biophys J
September 2024
Department of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.
The significant effects of lipid binding on the functionality of potassium channel KcsA have been validated by brilliant studies. However, the specific interactions between lipids and KcsA, such as binding parameters for each binding event, have not been fully elucidated. In this study, we employed native mass spectrometry to investigate the binding of lipids to KcsA and their effects on the channel.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!