Dataset Information

A molecular model of sea urchin reversible adhesion based on quantitative proteomics

ABSTRACT: Marine bioadhesives have unmatched performances especially in wet environments, being valuable sources of inspiration for industrial and biomedical applications. In sea urchins specialized adhesive organs, called tube feet, mediate adhesion. These are composed by a disc, which produces adhesive and de-adhesive secretions for strong reversible attachment, and a motile stem. After detachment, the secreted adhesive remains bound to the substratum as a footprint. Previous studies showed that sea urchin adhesive is composed of proteins and sugars, but so far only one protein, Nectin, was shown to be over-expressed as a transcript in tube feet discs, suggesting its involvement in sea urchin adhesion. Here we use high-resolution quantitative mass-spectrometry technologies to profile Paracentrotus lividus tube feet differential proteome, comparing protein expression levels in its adhesive part (disc) versus the non-adhesive part (stem). This allowed us to identify 163 highly over-expressed disc proteins and propose the first molecular model of sea urchin reversible adhesion. The secreted adhesive proteome was also analyzed, whereby we found that 70% of its components fall within five protein groups, involved in adhesive exocytosis and protection against microbes. Our data also provides evidence that Nectin is not only highly expressed in tube feet discs but is a component of the adhesive itself, thus constituting the first report of a sea urchin tube foot adhesive protein. These results give us an unprecedented insight on the molecular mechanics underlying sea urchins reversible adhesion, opening new doors to develop new, wet-reliable, reversible, efficient, ecological biomimetic adhesives.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Paracentrotus Lividus (common Sea Urchin)

SUBMITTER: Nicolas Lebesgue

LAB HEAD: Albert J.R Heck

PROVIDER: PXD003122 | Pride | 2016-03-21

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20141204_paracentrotus_lividus_SCX_disc.dat	Other
	20141204_paracentrotus_lividus_SCX_disc.mgf	Mgf
	20141204_paracentrotus_lividus_SCX_disc.xml	Xml
	20141204_paracentrotus_lividus_SCX_stem.dat	Other
	20141204_paracentrotus_lividus_SCX_stem.mgf	Mgf

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Publications

Deciphering the molecular mechanisms underlying sea urchin reversible adhesion: A quantitative proteomics approach.

Lebesgue Nicolas N da Costa Gonçalo G Ribeiro Raquel Mesquita RM Ribeiro-Silva Cristina C Martins Gabriel G GG Matranga Valeria V Scholten Arjen A Cordeiro Carlos C Heck Albert J R AJ Santos Romana R

Journal of proteomics 20160227

<h4>Unlabelled</h4>Marine bioadhesives have unmatched performances in wet environments, being an inspiration for biomedical applications. In sea urchins specialized adhesive organs, tube feet, mediate reversible adhesion, being composed by a disc, producing adhesive and de-adhesive secretions, and a motile stem. After tube foot detachment, the secreted adhesive remains bound to the substratum as a footprint. Sea urchin adhesive is composed by proteins and sugars, but so far only one protein, Nec ...[more]

PMID: 26926440

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Project description:Purpose: The Tbrain transcription factor has demonstrated an evolved preference for low-affinity, secondary site binding motifs between the sea star and sea urchin orthologs. We sought to identify targets of sea urchin and sea star orthologs of Tbr. Because less is known about the function of Tbr during sea star development, we used RNA-seq in conjuction with ChIP-seq studies (GEO:xxxx) to determine the targets of sea star Tbr in early development. Methods: Sea star (Patiria miniata) embryos were injected with translation-blocking morpholino antisense oligonucleotides to knock-down PmTbr expression, as described previously. Control morpholinos were injected into sibling embryos. Embryos were allowed to develop until hatching (30-36 hpf) at which point injected embryos were collected and RNA was extracted. RNA-seq libraries were prepared, sequenced, and analyzed using standard protocols. Results: There are 2,562 genes that are significantly differentially expressed relative to control morpholino inected embryos (FDR < 0.05). There are roughly equivalent numbers of genes down-regulated (1,041) and up-regulated (1,521) by Pm-tbr knockdown, suggesting that PmTbr may act as both a transcriptional activator and repressor. 1,165 differentially expressed genes are located within 75 kb of a PmTbr binding site determined using ChIP-seq, and this set is used as a basis for comparison between sea star and sea urchin binding sites. Conclusions: 1,165 targets of the PmTbr transcription factor were identified based on differential expression following knockdown and the presence of transcription factor binding sites proximal to differentially expressed genes. There are an equal number of up- and down-regulated targets, suggesting Tbr may function as a transcriptional activator and repressor, depending on context and target gene. There was no clear association of motif utilization with either the direction of differential expression or ontological category of the target gene. There are only a small fraction of target genes (approximately 10%) that are in common between the sea star and sea urchin sets.