ArticleThe Journal of biological chemistry2014
Identification of ligand specificity determinants in lantibiotic bovicin HJ50 and the receptor BovK, a multitransmembrane histidine kinase.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Complete Genome Sequencing Revealed the Potential Application of a NovelFoods (Basel, Switzerland) · 2023Article
- Mechanism of Action of Ribosomally Synthesized and Post-Translationally Modified Peptides.Chemical reviews · 2022Review
- Substrate Sequence Controls Regioselectivity of Lanthionine Formation by ProcM.Journal of the American Chemical Society · 2021Article
- CerR, a Single-Domain Regulatory Protein of the LuxR Family, Promotes Cerecidin Production and Immunity in Bacillus cereus.Applied and environmental microbiology · 2018Article
- Identification of Key Residues in the NisK Sensor Region for Nisin Biosynthesis Regulation.Frontiers in microbiology · 2017Article
- Type IV pilins regulate their own expression via direct intramembrane interactions with the sensor kinase PilS.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The journey of nisin development in China, a natural-green food preservative.Protein & cell · 2015Article
- Bovicin HJ50-like lantibiotics, a novel subgroup of lantibiotics featured by an indispensable disulfide bridge.PloS one · 2014Article
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Authors and funding
8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Lantibiotic bovicin HJ50 is produced by Streptococcus bovis HJ50 and acts as the extracellular signal to autoregulate its own biosynthesis through BovK/R two-component system. Bovicin HJ50 shows a linear N-terminal and glubolar C-terminal structure, and the sensor histidine kinase BovK contains eight transmembrane segments lacking any extensive surface-exposed sensory domain. The signal recognition mechanism between bovicin HJ50 and BovK is still unknown. We performed saturated alanine scanning mutagenesis and other amino acid substitutions on bovicin HJ50 using a semi-in vitro biosynthesis. Results of the mutants inducing activities indicated that several charged and hydrophobic amino acids in ring B of bovicin HJ50, as well as two glycines were key residues to recognize BovK. Circular dichroism analyses indicated that both glycines contributed to bovicin HJ50 structural changes in the membrane. Biotin-labeled bovicin HJ50 could interact with the N-terminal sensor of BovK, and several charged residues and a conserved hydrophobic region in the N-terminal portion of BovK sensor domain were important for interacting with the signal bovicin HJ50. By combining the results, we suggested a mechanism of bovicin HJ50 recognizing and activating BovK mainly through electrostatic and hydrophobic interactions.
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