Perna viridis
Ontology highlight
ABSTRACT:
PROVIDER: PRJDB10567 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| Other | ||||
| DRR244974_1.fastq.gz | Fastqsanger.gz | |||
| DRR244974_2.fastq.gz | Fastqsanger.gz | |||
| DRR244975_1.fastq.gz | Fastqsanger.gz | |||
| DRR244975_2.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 25 |
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Project description:Gill Specific Transcriptome Of Asian Green Mussel Perna viridis
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Project description:Transcriptomics reveal triphenyltin-induced molecular toxicity in the marine mussel Perna viridis
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Project description:Mollusk secretes a periostracum layer prior to the underlying calcified shell. This organic membrane serves as the first line of protection and primary template for shell orchestration. However, the chemical composition and formation mechanism of the periostracum layer is largely unknown. In this study, we applied transcriptomic, proteomics, physical and chemical analysis to unravel the mysteries of the periostracum formation in the green mussel Perna viridis (Linnaeus). Scanning electron microscopy examination and FTIR analysis showed that the periostracum layer was a multilayered organic membrane composed of polysaccharides, lipids and proteins. Interestingly, proteomic study identified components enriched in tyrosine and some enzymes evolved in tyrosine oxidation, indicating that tyrosine oxidation might play an important role in the periostracum formation. Moreover, comparative transcriptomics suggested that tyrosine-rich proteins were intensively synthesize in the periostracum groove. After being secreted, the periostracum proteins were gradually tanned by oxidation in the sea water, and the level of crosslink increased significantly as revealed by the ATR-FTIR. Our present study sheds light on the chemical composition and putative tanning mechanism of the periostracum layer in bivalve mollusk.
2022-10-20 | GSE215890 | GEO
Project description:For understanding the structural characteristics and the proteome of Perna shell, the microstructure, polymorph, and protein composition of the adult Perna viridis shell were investigated. The P. viridis shell have two distinct mineral layers, myostracum and nacre, with the same calcium carbonate polymorph of aragonite, determined by scanning electron microscope, Fourier transform infrared spectroscopy, and x-ray crystalline diffraction. Using Illumina sequencing, the mantle transcriptome of P. viridis was investigated and a total of 69,859 unigenes was generated. Using a combined proteomic/transcriptomic approach, a total of 378 shell proteins from P. viridis shell were identified, in which, 132 shell proteins identified with more than two matched unique peptides. Of the 132 shell proteins, 69 are exclusive to the nacre, 12 to the myostracum, and 51 are shared by both. The Myosin-tail domain containing proteins, Filament-like proteins, and Chitin-binding domain containing proteins represent the most abundant molecules. In addition, the shell matrix proteins (SMPs) containing biomineralization-related domains, such as Kunitz, A2M, WAP, EF-hand, PDZ, VWA, Collagen domain, and low complexity regions with abundant certain amino acids, were also identified from P. viridis shell. Collagenase and chitinase degradation can significantly change the morphology of the shell, indicating the important roles of collagen and chitin in the shell formation and the muscle-shell attachment. Our results present for the first time the proteome of P. viridis shell and increase the knowledge of SMPs in this genus.
| S-EPMC6641155 | biostudies-literature
Project description:The 3,4-dihydroxyphenyl-l-alanine (Dopa)-containing proteins of mussel byssus play a critical role in wet adhesion and have inspired versatile new synthetic strategies for adhesives and coatings. Apparently, however, not all mussel adhesive proteins are beholden to Dopa chemistry. The cDNA-deduced sequence of Pvfp-1, a highly aromatic and redox active byssal coating protein in the green mussel Perna viridis, suggests that Dopa may be replaced by a post-translational modification of tryptophan. The N-terminal tryptophan-rich domain of Pvfp-1 contains 42 decapeptide repeats with the consensus sequences ATPKPW(1)TAW(2)K and APPPAW(1)TAW(2)K. A small collagen domain (18 Gly-X-Y repeats) is also present. Tandem mass spectrometry of isolated tryptic decapeptides has detected both C(2)-hexosylated tryptophan (W(1)) and C(2)-hexosylated hydroxytryptophan (W(2)), the latter of which is redox active. The UV absorbance spectrum of W(2) is consistent with 7-hydroxytryptophan, which represents an intriguing new theme for bioinspired opportunistic wet adhesion.
| S-EPMC2749108 | biostudies-literature
Project description:Here, we integrated high-throughput transcriptome and proteome sequencing to construct a comprehensive protein database for the byssus of Chinese green mussel (Perna viridis), aiming at providing novel insights into the molecular mechanisms of byssal binding to heavy metals.
2019-04-30 | PXD009183 | Pride