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Functional shell matrix proteins tentatively identified by asymmetric snail shell morphology
Molluscan shell matrix proteins (SMPs) are essential in biomineralization. Here, we identify potentially important SMPs by exploiting the asymmetric shell growth in snail, Lymnaea stagnalis. Asymmetric shells require bilaterally asymmetric expression of SMP genes. We examined expression levels of 35...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7299971/ https://www.ncbi.nlm.nih.gov/pubmed/32555253 http://dx.doi.org/10.1038/s41598-020-66021-w |
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author | Ishikawa, Akito Shimizu, Keisuke Isowa, Yukinobu Takeuchi, Takeshi Zhao, Ran Kito, Keiji Fujie, Manabu Satoh, Noriyuki Endo, Kazuyoshi |
author_facet | Ishikawa, Akito Shimizu, Keisuke Isowa, Yukinobu Takeuchi, Takeshi Zhao, Ran Kito, Keiji Fujie, Manabu Satoh, Noriyuki Endo, Kazuyoshi |
author_sort | Ishikawa, Akito |
collection | PubMed |
description | Molluscan shell matrix proteins (SMPs) are essential in biomineralization. Here, we identify potentially important SMPs by exploiting the asymmetric shell growth in snail, Lymnaea stagnalis. Asymmetric shells require bilaterally asymmetric expression of SMP genes. We examined expression levels of 35,951 transcripts expressed in the left and right sides of mantle tissue of the pond snail, Lymnaea stagnalis. This transcriptome dataset was used to identify 207 SMPs by LC-MS/MS. 32 of the 207 SMP genes show asymmetric expression patterns, which were further verified for 4 of the 32 SMPs using quantitative PCR analysis. Among asymmetrically expressed SMPs in dextral snails, those that are more highly expressed on the left side than the right side are 3 times more abundant than those that are more highly expressed on the right than the left, suggesting potentially inhibitory roles of SMPs in shell formation. The 32 SMPs thus identified have distinctive features, such as conserved domains and low complexity regions, which may be essential in biomineralization. |
format | Online Article Text |
id | pubmed-7299971 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-72999712020-06-18 Functional shell matrix proteins tentatively identified by asymmetric snail shell morphology Ishikawa, Akito Shimizu, Keisuke Isowa, Yukinobu Takeuchi, Takeshi Zhao, Ran Kito, Keiji Fujie, Manabu Satoh, Noriyuki Endo, Kazuyoshi Sci Rep Article Molluscan shell matrix proteins (SMPs) are essential in biomineralization. Here, we identify potentially important SMPs by exploiting the asymmetric shell growth in snail, Lymnaea stagnalis. Asymmetric shells require bilaterally asymmetric expression of SMP genes. We examined expression levels of 35,951 transcripts expressed in the left and right sides of mantle tissue of the pond snail, Lymnaea stagnalis. This transcriptome dataset was used to identify 207 SMPs by LC-MS/MS. 32 of the 207 SMP genes show asymmetric expression patterns, which were further verified for 4 of the 32 SMPs using quantitative PCR analysis. Among asymmetrically expressed SMPs in dextral snails, those that are more highly expressed on the left side than the right side are 3 times more abundant than those that are more highly expressed on the right than the left, suggesting potentially inhibitory roles of SMPs in shell formation. The 32 SMPs thus identified have distinctive features, such as conserved domains and low complexity regions, which may be essential in biomineralization. Nature Publishing Group UK 2020-06-17 /pmc/articles/PMC7299971/ /pubmed/32555253 http://dx.doi.org/10.1038/s41598-020-66021-w Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Ishikawa, Akito Shimizu, Keisuke Isowa, Yukinobu Takeuchi, Takeshi Zhao, Ran Kito, Keiji Fujie, Manabu Satoh, Noriyuki Endo, Kazuyoshi Functional shell matrix proteins tentatively identified by asymmetric snail shell morphology |
title | Functional shell matrix proteins tentatively identified by asymmetric snail shell morphology |
title_full | Functional shell matrix proteins tentatively identified by asymmetric snail shell morphology |
title_fullStr | Functional shell matrix proteins tentatively identified by asymmetric snail shell morphology |
title_full_unstemmed | Functional shell matrix proteins tentatively identified by asymmetric snail shell morphology |
title_short | Functional shell matrix proteins tentatively identified by asymmetric snail shell morphology |
title_sort | functional shell matrix proteins tentatively identified by asymmetric snail shell morphology |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7299971/ https://www.ncbi.nlm.nih.gov/pubmed/32555253 http://dx.doi.org/10.1038/s41598-020-66021-w |
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