Dataset Information

Complexity of Yolk Proteins and Their Dynamics in the Sea Star Patiria miniata.

ABSTRACT: Oviparous animals store yolk proteins within the developing oocyte. These proteins are used in gametogenesis and as a nutritional source for embryogenesis. Vitellogenin and the major yolk protein are two of the most important yolk proteins among diverse species of invertebrates and vertebrates. Among the echinoderms, members of the subphyla Echinozoa (sea urchins and sea cucumbers) express the major yolk protein (MYP) but not vitellogenin (Vtg), while an initial report has documented that two Asterozoa (sea stars) express a vitellogenin. Our results show that sea stars contain two vitellogenins, Vtg 1 and Vtg 2, and MYP. In Patiria miniata, these genes are differentially expressed in the somatic and germ cells of the ovary: Vtg 1 is enriched in the somatic cells of the ovary but not in the oocytes, and Vtg 2 accumulates in both oocytes and somatic cells; MYP is not robustly present in either. Remarkably, Vtg 2 and MYP mRNA reappear in larvae; Vtg 2 is detected within cells of the ectoderm, and MYP accumulates in the coelomic pouches, the intestine, and the posterior enterocoel (PE), the site of germ line formation in this animal. Additionally, the Vtg 2 protein is present in oocytes, follicle cells, and developing embryos, but becomes undetectable following gastrulation. These results help elucidate the mechanisms involved in yolk dynamics, and provide molecular information that allows for greater understanding of the evolution of these important gene products.

SUBMITTER: Zazueta-Novoa V

PROVIDER: S-EPMC5103698 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature

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Complexity of Yolk Proteins and Their Dynamics in the Sea Star Patiria miniata.

Zazueta-Novoa Vanesa V Onorato Thomas M TM Reyes Gerardo G Oulhen Nathalie N Wessel Gary M GM

The Biological bulletin 20160601 3

Oviparous animals store yolk proteins within the developing oocyte. These proteins are used in gametogenesis and as a nutritional source for embryogenesis. Vitellogenin and the major yolk protein are two of the most important yolk proteins among diverse species of invertebrates and vertebrates. Among the echinoderms, members of the subphyla Echinozoa (sea urchins and sea cucumbers) express the major yolk protein (MYP) but not vitellogenin (Vtg), while an initial report has documented that two As ...[more]

PMID: 27365416

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Project description:BackgroundProteomic studies of skeletal proteins have revealed large, complex mixtures of proteins occluded within the mineral. Many skeletal proteomes contain rapidly evolving proteins with repetitive domains, further complicating our understanding. In echinoderms, proteomic analysis of the skeletal proteomes of mineralized tissues of the sea urchin Strongylocentrotus purpuratus prominently featured spicule matrix proteins with repetitive sequences linked to a C-type lectin domain. A comparative study of the brittle star Ophiocoma wendtii skeletal proteome revealed an order of magnitude fewer proteins containing C-type lectin domains. A number of other proteins conserved in the skeletons of the two groups were identified. Here we report the complete skeletal proteome of the sea star Patiria miniata and compare it to that of the other echinoderm groups.ResultsWe have identified eighty-five proteins in the P. miniata skeletal proteome. Forty-two percent of the proteins were determined to be homologous to proteins found in the S. purpuratus skeletal proteomes. An additional 34 % were from similar functional classes as proteins in the urchin proteomes. Thirteen percent of the P. miniata proteins had homologues in the O. wendtii skeletal proteome with an additional 29% showing similarity to brittle star skeletal proteins. The P. miniata skeletal proteome did not contain any proteins with C-lectin domains or with acidic repetitive regions similar to the sea urchin or brittle star spicule matrix proteins. MSP130 proteins were also not found. We did identify a number of proteins homologous between the three groups. Some of the highly conserved proteins found in echinoderm skeletons have also been identified in vertebrate skeletons.ConclusionsThe presence of proteins conserved in the skeleton in three different echinoderm groups indicates these proteins are important in skeleton formation. That a number of these proteins are involved in skeleton formation in vertebrates suggests a common origin for some of the fundamental processes co-opted for skeleton formation in deuterostomes. The proteins we identify suggest transport of proteins and calcium via endosomes was co-opted to this function in a convergent fashion. Our data also indicate that modifications to the process of skeleton formation can occur through independent co-option of proteins following species divergence as well as through domain shuffling.

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.

Dataset Information

Complexity of Yolk Proteins and Their Dynamics in the Sea Star Patiria miniata.

Publications

Complexity of Yolk Proteins and Their Dynamics in the Sea Star Patiria miniata.

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