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Identification and Characterization of a Novel Family of Cysteine-Rich Peptides (MgCRP-I) from Mytilus galloprovincialis.

Gerdol M, Puillandre N, De Moro G, Guarnaccia C, Lucafò M, Benincasa M, Zlatev V, Manfrin C, Torboli V, Giulianini PG, Sava G, Venier P, Pallavicini A - Genome Biol Evol (2015)

Bottom Line: Genome- and transcriptome-wide searches for orthologous sequences in other bivalve species indicated the unique presence of this gene family in Mytilus spp.Like many antimicrobial peptides and neurotoxins, MgCRP-I peptides are produced as pre-propeptides, usually have a net positive charge and likely derive from similar evolutionary mechanisms, that is, gene duplication and positive selection within the mature peptide region; however, synthetic MgCRP-I peptides did not display significant toxicity in cultured mammalian cells, insecticidal, antimicrobial, or antifungal activities.The functional role of MgCRP-I peptides in mussel physiology still remains puzzling.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Sciences, University of Trieste, Italy.

No MeSH data available.


Related in: MedlinePlus

Maximum-likelihood tree obtained with the MgCRP-I peptides based on the alignment of the signal peptide region only. Only bootstraps values greater than 75 are shown. Some sequences were not considered in this analysis as their N-terminal region was incomplete (see table 2). Arrows indicate two MgCRP-I-like peptides with a disrupted cysteine array (MgCRP-I 12 and 23), marking an unconventional mature region.
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evv133-F3: Maximum-likelihood tree obtained with the MgCRP-I peptides based on the alignment of the signal peptide region only. Only bootstraps values greater than 75 are shown. Some sequences were not considered in this analysis as their N-terminal region was incomplete (see table 2). Arrows indicate two MgCRP-I-like peptides with a disrupted cysteine array (MgCRP-I 12 and 23), marking an unconventional mature region.

Mentions: The combined genomic/transcriptomic analyses indicate the presence of at least 67 different potentially functional CRP-I loci in the genome of the Mediterranean mussel. Owing to the preliminary nature of the released mussel genome (Nguyen et al. 2014), this has to be considered as a conservative estimate. The phylogenetic analysis of the CRP-I signal peptide regions (fig. 3) evidenced the existence of several highly similar paralogous genes, highlighting the important role of gene duplication events in the evolution of the MgCRP-I gene family, which in some cases appear to have occurred very recently (supplementary fig. S4, Supplementary Material online). A number of MgCRP-I pseudogenes with frameshift or missense mutations were identified in the mussel genome (supplementary table S5, Supplementary Material online) and, at the same time, the frequent sequence truncations caused by the small size of the genomic contigs make impossible to infer how many of the incomplete MgCRP-I loci are fully functional (see table 2). For the same reason, the presence of common regulatory regions and transposable elements which could have driven the expansion of this gene family will be matter of future investigations.Fig. 3.—


Identification and Characterization of a Novel Family of Cysteine-Rich Peptides (MgCRP-I) from Mytilus galloprovincialis.

Gerdol M, Puillandre N, De Moro G, Guarnaccia C, Lucafò M, Benincasa M, Zlatev V, Manfrin C, Torboli V, Giulianini PG, Sava G, Venier P, Pallavicini A - Genome Biol Evol (2015)

Maximum-likelihood tree obtained with the MgCRP-I peptides based on the alignment of the signal peptide region only. Only bootstraps values greater than 75 are shown. Some sequences were not considered in this analysis as their N-terminal region was incomplete (see table 2). Arrows indicate two MgCRP-I-like peptides with a disrupted cysteine array (MgCRP-I 12 and 23), marking an unconventional mature region.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4558851&req=5

evv133-F3: Maximum-likelihood tree obtained with the MgCRP-I peptides based on the alignment of the signal peptide region only. Only bootstraps values greater than 75 are shown. Some sequences were not considered in this analysis as their N-terminal region was incomplete (see table 2). Arrows indicate two MgCRP-I-like peptides with a disrupted cysteine array (MgCRP-I 12 and 23), marking an unconventional mature region.
Mentions: The combined genomic/transcriptomic analyses indicate the presence of at least 67 different potentially functional CRP-I loci in the genome of the Mediterranean mussel. Owing to the preliminary nature of the released mussel genome (Nguyen et al. 2014), this has to be considered as a conservative estimate. The phylogenetic analysis of the CRP-I signal peptide regions (fig. 3) evidenced the existence of several highly similar paralogous genes, highlighting the important role of gene duplication events in the evolution of the MgCRP-I gene family, which in some cases appear to have occurred very recently (supplementary fig. S4, Supplementary Material online). A number of MgCRP-I pseudogenes with frameshift or missense mutations were identified in the mussel genome (supplementary table S5, Supplementary Material online) and, at the same time, the frequent sequence truncations caused by the small size of the genomic contigs make impossible to infer how many of the incomplete MgCRP-I loci are fully functional (see table 2). For the same reason, the presence of common regulatory regions and transposable elements which could have driven the expansion of this gene family will be matter of future investigations.Fig. 3.—

Bottom Line: Genome- and transcriptome-wide searches for orthologous sequences in other bivalve species indicated the unique presence of this gene family in Mytilus spp.Like many antimicrobial peptides and neurotoxins, MgCRP-I peptides are produced as pre-propeptides, usually have a net positive charge and likely derive from similar evolutionary mechanisms, that is, gene duplication and positive selection within the mature peptide region; however, synthetic MgCRP-I peptides did not display significant toxicity in cultured mammalian cells, insecticidal, antimicrobial, or antifungal activities.The functional role of MgCRP-I peptides in mussel physiology still remains puzzling.

View Article: PubMed Central - PubMed

Affiliation: Department of Life Sciences, University of Trieste, Italy.

No MeSH data available.


Related in: MedlinePlus