Reference - Detail
| RRC ID | 34328 |
|---|---|
| Author | Miyamoto KT, Komatsu M, Ikeda H. |
| Title | Discovery of gene cluster for mycosporine-like amino acid biosynthesis from Actinomycetales microorganisms and production of a novel mycosporine-like amino acid by heterologous expression. |
| Journal | Appl Environ Microbiol |
| Abstract |
Mycosporines and mycosporine-like amino acids (MAAs), including shinorine (mycosporine-glycine-serine) and porphyra-334 (mycosporine-glycine-threonine), are UV-absorbing compounds produced by cyanobacteria, fungi, and marine micro- and macroalgae. These MAAs have the ability to protect these organisms from damage by environmental UV radiation. Although no reports have described the production of MAAs and the corresponding genes involved in MAA biosynthesis from Gram-positive bacteria to date, genome mining of the Gram-positive bacterial database revealed that two microorganisms belonging to the order Actinomycetales, Actinosynnema mirum DSM 43827 and Pseudonocardia sp. strain P1, possess a gene cluster homologous to the biosynthetic gene clusters identified from cyanobacteria. When the two strains were grown in liquid culture, Pseudonocardia sp. accumulated a very small amount of MAA-like compound in a medium-dependent manner, whereas A. mirum did not produce MAAs under any culture conditions, indicating that the biosynthetic gene cluster of A. mirum was in a cryptic state in this microorganism. In order to characterize these biosynthetic gene clusters, each biosynthetic gene cluster was heterologously expressed in an engineered host, Streptomyces avermitilis SUKA22. Since the resultant transformants carrying the entire biosynthetic gene cluster controlled by an alternative promoter produced mainly shinorine, this is the first confirmation of a biosynthetic gene cluster for MAA from Gram-positive bacteria. Furthermore, S. avermitilis SUKA22 transformants carrying the biosynthetic gene cluster for MAA of A. mirum accumulated not only shinorine and porphyra-334 but also a novel MAA. Structure elucidation revealed that the novel MAA is mycosporine-glycine-alanine, which substitutes l-alanine for the l-serine of shinorine. |
| Volume | 80(16) |
| Pages | 5028-36 |
| Published | 2014-8-1 |
| DOI | 10.1128/AEM.00727-14 |
| PII | AEM.00727-14 |
| PMID | 24907338 |
| PMC | PMC4135781 |
| MeSH | Actinomycetales / genetics* Actinomycetales / metabolism Amino Acids / biosynthesis* Bacterial Proteins / genetics* Bacterial Proteins / metabolism Cyclohexanones Cyclohexylamines Gene Expression* Glycine / analogs & derivatives* Glycine / biosynthesis Multigene Family* Streptomyces / genetics Streptomyces / metabolism* |
| IF | 4.016 |
| Times Cited | 35 |
| WOS Category | BIOTECHNOLOGY & APPLIED MICROBIOLOGY MICROBIOLOGY |
| Altmetric score |
オルトメトリクス指標項目
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| The most frequently cited source | Patent(IFI CLAIMS) |
| Total number of mentions | 7 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| General Microbes | JCM 3225 |