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Cyanobactins from Cyanobacteria: Current Genetic and Chemical State of Knowledge.

Martins J, Vasconcelos V - Mar Drugs (2015)

Bottom Line: Apart from non-ribosomal peptides and polyketides, ribosomally synthesized and post-translationally modified peptides (RiPPs) are one of the leading groups of bioactive compounds produced by cyanobacteria.It is assumed that the primary source of cyanobactins is cyanobacteria, although these compounds have also been isolated from marine animals such as ascidians, sponges and mollusks.The aim of this review is to update the current knowledge of cyanobactins, recognized as being produced by cyanobacteria, and to emphasize their genetic clusters and chemical structures as well as their bioactivities, ecological roles and biotechnological potential.

View Article: PubMed Central - PubMed

Affiliation: Faculty of Sciences, University of Porto, Rua do Campo Alegre, Porto 4169-007, Portugal. joana.o.martins@gmail.com.

ABSTRACT
Cyanobacteria are considered to be one of the most promising sources of new, natural products. Apart from non-ribosomal peptides and polyketides, ribosomally synthesized and post-translationally modified peptides (RiPPs) are one of the leading groups of bioactive compounds produced by cyanobacteria. Among these, cyanobactins have sparked attention due to their interesting bioactivities and for their potential to be prospective candidates in the development of drugs. It is assumed that the primary source of cyanobactins is cyanobacteria, although these compounds have also been isolated from marine animals such as ascidians, sponges and mollusks. The aim of this review is to update the current knowledge of cyanobactins, recognized as being produced by cyanobacteria, and to emphasize their genetic clusters and chemical structures as well as their bioactivities, ecological roles and biotechnological potential.

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Cyanobactins that do not encode heterocyclization or oxidationenzymes. Thepeptides are organized in chronological order and the sequence of the core peptide is presented in linear form. The location of the prenyl group is indicated by one-letter amino acid abbreviation in the corresponding column. The genes are identified by different colors. Prenylation (pale red) is indicated in the chemical structure.
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marinedrugs-13-06910-f005: Cyanobactins that do not encode heterocyclization or oxidationenzymes. Thepeptides are organized in chronological order and the sequence of the core peptide is presented in linear form. The location of the prenyl group is indicated by one-letter amino acid abbreviation in the corresponding column. The genes are identified by different colors. Prenylation (pale red) is indicated in the chemical structure.

Mentions: The whole genome sequence from the strain Anabaena sp. 90 allowed for the discovery of new cyanobactins, designated anacyclamides by Leikoski and colleagues [20]. Using bioinformatics tools coupled with stable isotope labeling and MS, these novel cyclic peptides were found in a total of 27 Anabaena strains. Anacyclamides can differ from 7 to 20 amino acids in length, enclosing only proteinogenic amino acids that can be prenylated or geranylated. The acy gene cluster (~10.7 kb) is composed of 11 genes organized bidirectionally, such as in the trichamide gene cluster. Only one precursor peptide gene is present in the acy genetic cluster. Nevertheless, 15 distinct amino acid sequences from the core peptide were detected from 27 strains yielding 18 unique anacyclamides. The acy gene cluster lacks acyD as well as an oxidase domain, which is consistent with the chemical structure of these metabolites. In contrast to the other reported cyanobactins, anacyclamides exhibit a pronounced amino acid variation with only one proline at the conserved C-terminus [20]. With the discovery of anacyclamides, the definition of cyanobactins was extended to include unmodified peptides that can have prenylated or geranylated amino acids (Figure 5).


Cyanobactins from Cyanobacteria: Current Genetic and Chemical State of Knowledge.

Martins J, Vasconcelos V - Mar Drugs (2015)

Cyanobactins that do not encode heterocyclization or oxidationenzymes. Thepeptides are organized in chronological order and the sequence of the core peptide is presented in linear form. The location of the prenyl group is indicated by one-letter amino acid abbreviation in the corresponding column. The genes are identified by different colors. Prenylation (pale red) is indicated in the chemical structure.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4663559&req=5

marinedrugs-13-06910-f005: Cyanobactins that do not encode heterocyclization or oxidationenzymes. Thepeptides are organized in chronological order and the sequence of the core peptide is presented in linear form. The location of the prenyl group is indicated by one-letter amino acid abbreviation in the corresponding column. The genes are identified by different colors. Prenylation (pale red) is indicated in the chemical structure.
Mentions: The whole genome sequence from the strain Anabaena sp. 90 allowed for the discovery of new cyanobactins, designated anacyclamides by Leikoski and colleagues [20]. Using bioinformatics tools coupled with stable isotope labeling and MS, these novel cyclic peptides were found in a total of 27 Anabaena strains. Anacyclamides can differ from 7 to 20 amino acids in length, enclosing only proteinogenic amino acids that can be prenylated or geranylated. The acy gene cluster (~10.7 kb) is composed of 11 genes organized bidirectionally, such as in the trichamide gene cluster. Only one precursor peptide gene is present in the acy genetic cluster. Nevertheless, 15 distinct amino acid sequences from the core peptide were detected from 27 strains yielding 18 unique anacyclamides. The acy gene cluster lacks acyD as well as an oxidase domain, which is consistent with the chemical structure of these metabolites. In contrast to the other reported cyanobactins, anacyclamides exhibit a pronounced amino acid variation with only one proline at the conserved C-terminus [20]. With the discovery of anacyclamides, the definition of cyanobactins was extended to include unmodified peptides that can have prenylated or geranylated amino acids (Figure 5).

Bottom Line: Apart from non-ribosomal peptides and polyketides, ribosomally synthesized and post-translationally modified peptides (RiPPs) are one of the leading groups of bioactive compounds produced by cyanobacteria.It is assumed that the primary source of cyanobactins is cyanobacteria, although these compounds have also been isolated from marine animals such as ascidians, sponges and mollusks.The aim of this review is to update the current knowledge of cyanobactins, recognized as being produced by cyanobacteria, and to emphasize their genetic clusters and chemical structures as well as their bioactivities, ecological roles and biotechnological potential.

View Article: PubMed Central - PubMed

Affiliation: Faculty of Sciences, University of Porto, Rua do Campo Alegre, Porto 4169-007, Portugal. joana.o.martins@gmail.com.

ABSTRACT
Cyanobacteria are considered to be one of the most promising sources of new, natural products. Apart from non-ribosomal peptides and polyketides, ribosomally synthesized and post-translationally modified peptides (RiPPs) are one of the leading groups of bioactive compounds produced by cyanobacteria. Among these, cyanobactins have sparked attention due to their interesting bioactivities and for their potential to be prospective candidates in the development of drugs. It is assumed that the primary source of cyanobactins is cyanobacteria, although these compounds have also been isolated from marine animals such as ascidians, sponges and mollusks. The aim of this review is to update the current knowledge of cyanobactins, recognized as being produced by cyanobacteria, and to emphasize their genetic clusters and chemical structures as well as their bioactivities, ecological roles and biotechnological potential.

Show MeSH
Related in: MedlinePlus