ArticleThe Journal of antibiotics2018
Identification of a novel bacteriocin-like protein and structural gene from Rhodococcus erythropolis JCM 2895, using suppression-subtractive hybridization.
Article in The Journal of antibiotics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Polyethylene Biodegradation by an Artificial Bacterial Consortium: Rhodococcus as a Competitive Plastisphere Species.Microbes and environments · 2024Article
- Development of Efficient Genome-Reduction Tool Based on Cre/Microorganisms · 2023Article
- Complete Genome Sequence of Rhodococcus erythropolis JCM 2895, an Antibiotic Protein-Producing Strain.Microbiology resource announcements · 2022Article
- Biotechnology of Rhodococcus for the production of valuable compounds.Applied microbiology and biotechnology · 2020Review
- Developing a codon optimization method for improved expression of recombinant proteins in actinobacteria.Scientific reports · 2019Article
- Current taxonomy of Rhodococcus species and their role in infections.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2018Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A novel bacteriocin-like protein and its structural gene (rap) were identified from Rhodococcus erythropolis JCM 2895. The rapA and B genes are located on a 5.4-kb circular plasmid, and were obtained using a modified suppression-subtractive hybridization method. The rapA and B genes were heterologously expressed in Rhodococcus sp. or Escherichia coli, and then characterized. The results indicated that RapA is a small, water-soluble, heat-stable antimicrobial protein, and that RapB is an immunity protein against RapA, estimated to be located on the cell membrane. RapA showed antimicrobial activity particularly against R. erythropolis, and the activity persisted even after SDS-PAGE analysis. For the heterologous expressed RapA protein, N-terminal amino acid sequence was also confirmed. This is the first report of a bacteriocin-like substance obtained from the genus Rhodococcus.
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