Dual Gene Repertoires for Larval and Adult Shells Reveal Molecules Essential for Molluscan Shell Formation. (31st August 2018)
- Record Type:
- Journal Article
- Title:
- Dual Gene Repertoires for Larval and Adult Shells Reveal Molecules Essential for Molluscan Shell Formation. (31st August 2018)
- Main Title:
- Dual Gene Repertoires for Larval and Adult Shells Reveal Molecules Essential for Molluscan Shell Formation
- Authors:
- Zhao, Ran
Takeuchi, Takeshi
Luo, Yi-Jyun
Ishikawa, Akito
Kobayashi, Tatsushi
Koyanagi, Ryo
Villar-Briones, Alejandro
Yamada, Lixy
Sawada, Hitoshi
Iwanaga, Shunsuke
Nagai, Kiyohito
Satoh, Noriyuki
Endo, Kazuyoshi - Editors:
- True, John
- Abstract:
- Abstract: Molluscan shells, mainly composed of calcium carbonate, also contain organic components such as proteins and polysaccharides. Shell organic matrices construct frameworks of shell structures and regulate crystallization processes during shell formation. To date, a number of shell matrix proteins (SMPs) have been identified, and their functions in shell formation have been studied. However, previous studies focused only on SMPs extracted from adult shells, secreted after metamorphosis. Using proteomic analyses combined with genomic and transcriptomic analyses, we have identified 31 SMPs from larval shells of the pearl oyster, Pinctada fucata, and 111 from the Pacific oyster, Crassostrea gigas . Larval SMPs are almost entirely different from those of adults in both species. RNA-seq data also confirm that gene expression profiles for larval and adult shell formation are nearly completely different. Therefore, bivalves have two repertoires of SMP genes to construct larval and adult shells. Despite considerable differences in larval and adult SMPs, some functional domains are shared by both SMP repertoires. Conserved domains include von Willebrand factor type A (VWA), chitin-binding (CB), carbonic anhydrase (CA), and acidic domains. These conserved domains are thought to play crucial roles in shell formation. Furthermore, a comprehensive survey of animal genomes revealed that the CA and VWA–CB domain-containing protein families expanded in molluscs after their separationAbstract: Molluscan shells, mainly composed of calcium carbonate, also contain organic components such as proteins and polysaccharides. Shell organic matrices construct frameworks of shell structures and regulate crystallization processes during shell formation. To date, a number of shell matrix proteins (SMPs) have been identified, and their functions in shell formation have been studied. However, previous studies focused only on SMPs extracted from adult shells, secreted after metamorphosis. Using proteomic analyses combined with genomic and transcriptomic analyses, we have identified 31 SMPs from larval shells of the pearl oyster, Pinctada fucata, and 111 from the Pacific oyster, Crassostrea gigas . Larval SMPs are almost entirely different from those of adults in both species. RNA-seq data also confirm that gene expression profiles for larval and adult shell formation are nearly completely different. Therefore, bivalves have two repertoires of SMP genes to construct larval and adult shells. Despite considerable differences in larval and adult SMPs, some functional domains are shared by both SMP repertoires. Conserved domains include von Willebrand factor type A (VWA), chitin-binding (CB), carbonic anhydrase (CA), and acidic domains. These conserved domains are thought to play crucial roles in shell formation. Furthermore, a comprehensive survey of animal genomes revealed that the CA and VWA–CB domain-containing protein families expanded in molluscs after their separation from other Lophotrochozoan linages such as the Brachiopoda. After gene expansion, some family members were co-opted for molluscan SMPs that may have triggered to develop mineralized shells from ancestral, nonmineralized chitinous exoskeletons. … (more)
- Is Part Of:
- Molecular biology and evolution. Volume 35:Number 11(2018)
- Journal:
- Molecular biology and evolution
- Issue:
- Volume 35:Number 11(2018)
- Issue Display:
- Volume 35, Issue 11 (2018)
- Year:
- 2018
- Volume:
- 35
- Issue:
- 11
- Issue Sort Value:
- 2018-0035-0011-0000
- Page Start:
- 2751
- Page End:
- 2761
- Publication Date:
- 2018-08-31
- Subjects:
- biomineralization -- larval shell -- mollusca -- proteome -- shell matrix protein
Molecular biology -- Periodicals
Molecular evolution -- Periodicals
Evolution, Molecular -- Periodicals
Molecular Biology -- Periodicals
572.8 - Journal URLs:
- http://mbe.oxfordjournals.org/ ↗
http://www.molbiolevol.org/ ↗
http://ukcatalogue.oup.com/ ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=0737-7038;screen=info;ECOIP ↗ - DOI:
- 10.1093/molbev/msy172 ↗
- Languages:
- English
- ISSNs:
- 0737-4038
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.782000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 24968.xml