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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...

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Autores principales: Ishikawa, Akito, Shimizu, Keisuke, Isowa, Yukinobu, Takeuchi, Takeshi, Zhao, Ran, Kito, Keiji, Fujie, Manabu, Satoh, Noriyuki, Endo, Kazuyoshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
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.
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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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