Limits...
Genome mining demonstrates the widespread occurrence of gene clusters encoding bacteriocins in cyanobacteria.

Wang H, Fewer DP, Sivonen K - PLoS ONE (2011)

Bottom Line: They ranged in length from 28 to 164 amino acids with very little sequence conservation of the core peptide.This classification is supported by phylogenetic analysis, which further indicated independent evolutionary trajectories of gene clusters in different groups.Our data suggests that cyanobacteria are a prolific source of low-molecular weight post-translationally modified peptides.

View Article: PubMed Central - PubMed

Affiliation: Division of Microbiology, Department of Food and Environment Sciences, University of Helsinki, Helsinki, Finland.

ABSTRACT
Cyanobacteria are a rich source of natural products with interesting biological activities. Many of these are peptides and the end products of a non-ribosomal pathway. However, several cyanobacterial peptide classes were recently shown to be produced through the proteolytic cleavage and post-translational modification of short precursor peptides. A new class of bacteriocins produced through the proteolytic cleavage and heterocyclization of precursor proteins was recently identified from marine cyanobacteria. Here we show the widespread occurrence of bacteriocin gene clusters in cyanobacteria through comparative analysis of 58 cyanobacterial genomes. A total of 145 bacteriocin gene clusters were discovered through genome mining. These clusters encoded 290 putative bacteriocin precursors. They ranged in length from 28 to 164 amino acids with very little sequence conservation of the core peptide. The gene clusters could be classified into seven groups according to their gene organization and domain composition. This classification is supported by phylogenetic analysis, which further indicated independent evolutionary trajectories of gene clusters in different groups. Our data suggests that cyanobacteria are a prolific source of low-molecular weight post-translationally modified peptides.

Show MeSH
Sequence logos of double-glycine motif generated from cyanobacterial precursors in NHLP and N11P families.There is a conserved region found near the peptide cleavage site with Gly-Gly motif from the precursor peptides. Relative frequency of acidic residues of the conserved sequences from families (A) NHLP and (B) N11P are demonstrated. This figure was generated by web-based software [39].
© Copyright Policy
Related In: Results  -  Collection


getmorefigures.php?uid=PMC3140520&req=5

pone-0022384-g003: Sequence logos of double-glycine motif generated from cyanobacterial precursors in NHLP and N11P families.There is a conserved region found near the peptide cleavage site with Gly-Gly motif from the precursor peptides. Relative frequency of acidic residues of the conserved sequences from families (A) NHLP and (B) N11P are demonstrated. This figure was generated by web-based software [39].

Mentions: Two protein families of double-glycine-type precursors, NHLP and N11P, were recently redefined [21]. A total of 121 identified precursors can be classified into these two families based on sequence similarity (Table 2). Sequence logos of double glycine motif generated from precursors in the two families display the conservation between them (Figure 3), and to the motif in other bacteria [20], [21]. Sequence alignments of the core peptides reveal a high level diversity both in size and amino acid composition with rich Gly, Cys, Ser and Thr residues that may undergo posttranslational modifications (Figure 4). Moreover, in this study, we also discovered 46 novel precursor proteins which are absent from the current genomic annotation (Table 2); eleven of them were grouped into NHLP and N11P families (Table S3).


Genome mining demonstrates the widespread occurrence of gene clusters encoding bacteriocins in cyanobacteria.

Wang H, Fewer DP, Sivonen K - PLoS ONE (2011)

Sequence logos of double-glycine motif generated from cyanobacterial precursors in NHLP and N11P families.There is a conserved region found near the peptide cleavage site with Gly-Gly motif from the precursor peptides. Relative frequency of acidic residues of the conserved sequences from families (A) NHLP and (B) N11P are demonstrated. This figure was generated by web-based software [39].
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3140520&req=5

pone-0022384-g003: Sequence logos of double-glycine motif generated from cyanobacterial precursors in NHLP and N11P families.There is a conserved region found near the peptide cleavage site with Gly-Gly motif from the precursor peptides. Relative frequency of acidic residues of the conserved sequences from families (A) NHLP and (B) N11P are demonstrated. This figure was generated by web-based software [39].
Mentions: Two protein families of double-glycine-type precursors, NHLP and N11P, were recently redefined [21]. A total of 121 identified precursors can be classified into these two families based on sequence similarity (Table 2). Sequence logos of double glycine motif generated from precursors in the two families display the conservation between them (Figure 3), and to the motif in other bacteria [20], [21]. Sequence alignments of the core peptides reveal a high level diversity both in size and amino acid composition with rich Gly, Cys, Ser and Thr residues that may undergo posttranslational modifications (Figure 4). Moreover, in this study, we also discovered 46 novel precursor proteins which are absent from the current genomic annotation (Table 2); eleven of them were grouped into NHLP and N11P families (Table S3).

Bottom Line: They ranged in length from 28 to 164 amino acids with very little sequence conservation of the core peptide.This classification is supported by phylogenetic analysis, which further indicated independent evolutionary trajectories of gene clusters in different groups.Our data suggests that cyanobacteria are a prolific source of low-molecular weight post-translationally modified peptides.

View Article: PubMed Central - PubMed

Affiliation: Division of Microbiology, Department of Food and Environment Sciences, University of Helsinki, Helsinki, Finland.

ABSTRACT
Cyanobacteria are a rich source of natural products with interesting biological activities. Many of these are peptides and the end products of a non-ribosomal pathway. However, several cyanobacterial peptide classes were recently shown to be produced through the proteolytic cleavage and post-translational modification of short precursor peptides. A new class of bacteriocins produced through the proteolytic cleavage and heterocyclization of precursor proteins was recently identified from marine cyanobacteria. Here we show the widespread occurrence of bacteriocin gene clusters in cyanobacteria through comparative analysis of 58 cyanobacterial genomes. A total of 145 bacteriocin gene clusters were discovered through genome mining. These clusters encoded 290 putative bacteriocin precursors. They ranged in length from 28 to 164 amino acids with very little sequence conservation of the core peptide. The gene clusters could be classified into seven groups according to their gene organization and domain composition. This classification is supported by phylogenetic analysis, which further indicated independent evolutionary trajectories of gene clusters in different groups. Our data suggests that cyanobacteria are a prolific source of low-molecular weight post-translationally modified peptides.

Show MeSH