ArticleDNA research : an international journal for rapid publication of reports on genes and genomes2017
Complete genome sequence and expression profile of the commercial lytic enzyme producer Lysobacter enzymogenes M497-1.
Article in DNA research : an international journal for rapid publication of reports on genes and genomes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 15 citations in OpenAlex.
- Dose-dependent effect of Bacillus subtilis on aquaculture pond ecosystems.World journal of microbiology & biotechnology · 2026Article
- Ultrahigh-throughput screening of environmental bacteria for proteolytic activity using droplet-based microfluidics.Applied and environmental microbiology · 2025Article
- A new bacteriolytic amidase Ami of Lysobacter capsici XL1.Scientific reports · 2025Article
- Reverse Osmosis in an Advanced Water Treatment Train Produces a Simple, Consistent Microbial Community.ACS ES&T engineering · 2025Article
- Diversity pattern and antibiotic activity of microbial communities inhabiting a karst cave from Costa Rica.Microbiology (Reading, England) · 2024Article
- Phylogenetic Revisit to a Review on Predatory Bacteria.Microorganisms · 2023Review
- The First Homologous Expression System for the β-Lytic Protease ofInternational journal of molecular sciences · 2022Article
- Comparative genomics provides insights into the potential biocontrol mechanism of twoFrontiers in microbiology · 2022Article
- Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering.Microbial cell factories · 2021Article
- β-Lytic Protease ofAntibiotics (Basel, Switzerland) · 2020Article
- Lytic potential of Lysobacter capsici VKM B-2533Scientific reports · 2020Article
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Authors and funding
10 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lysobacter enzymogenes M497-1 is a producer of commercialized achromopeptidase and is expected to harbour genes encoding various other antimicrobial enzymes. Here, we present the complete sequence of the genome of M497-1 and the expression profiles of the genes for various antimicrobial enzymes. Of the 117 peptidase-encoding genes found in the 6.1-Mb genome of M497-1, 15 genes (aside from the gene encoding the achromopeptidase) were expressed at a level higher than that of the average ribosomal protein genes in the 24-h culture. Thus, the strain was found more valuable than hitherto considered. In addition, M497-1 harbours 98 genes involved in the biosynthesis of various natural products, 16 of which are M497-1-specific across 4 Lysobacter species. A gene cluster starting at LEN_2603 through LEN_2673 among the 98 genes closely resembled the lysobactin biosynthesis gene cluster of Lysobacter sp. ATCC 53042. It is likely that M497-1 may produce lysobactin or related antibacterial compounds. Furthermore, comparative genomic analysis of M497-1 and four other Lysobacter species revealed that their core genome structure comprises 3,737 orthologous groups. Our findings are expected to advance further biotechnological application of Lysobacter spp. as a promising source of natural bioactive compounds.
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