Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix.

Mollusks shell formation is mediated by matrix proteins and many of these proteins have been identified and characterized. However, the mechanisms of protein control remain unknown. Here, we report the ubiquitylation of matrix proteins in the prismatic layer of the pearl oyster, Pinctada fucata. The...

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Autores principales:	Dong Fang, Cong Pan, Huijuan Lin, Ya Lin, Guangrui Xu, Guiyou Zhang, Hongzhong Wang, Liping Xie, Rongqing Zhang
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b53787dcd35d4de39d29e8c0f2fc2f2a
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spelling	oai:doaj.org-article:b53787dcd35d4de39d29e8c0f2fc2f2a2021-11-18T07:20:56ZUbiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix.1932-620310.1371/journal.pone.0035715https://doaj.org/article/b53787dcd35d4de39d29e8c0f2fc2f2a2012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22558208/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Mollusks shell formation is mediated by matrix proteins and many of these proteins have been identified and characterized. However, the mechanisms of protein control remain unknown. Here, we report the ubiquitylation of matrix proteins in the prismatic layer of the pearl oyster, Pinctada fucata. The presence of ubiquitylated proteins in the prismatic layer of the shell was detected with a combination of western blot and immunogold assays. The coupled ubiquitins were separated and identified by Edman degradation and liquid chromatography/mass spectrometry (LC/MS). Antibody injection in vivo resulted in large amounts of calcium carbonate randomly accumulating on the surface of the nacreous layer. These ubiquitylated proteins could bind to specific faces of calcite and aragonite, which are the two main mineral components of the shell. In the in vitro calcium carbonate crystallization assay, they could reduce the rate of calcium carbonate precipitation and induce the calcite formation. Furthermore, when the attached ubiquitins were removed, the functions of the EDTA-soluble matrix of the prismatic layer were changed. Their potency to inhibit precipitation of calcium carbonate was decreased and their influence on the morphology of calcium carbonate crystals was changed. Taken together, ubiquitylation is involved in shell formation. Although the ubiquitylation is supposed to be involved in every aspect of biophysical processes, our work connected the biomineralization-related proteins and the ubiquitylation mechanism in the extracellular matrix for the first time. This would promote our understanding of the shell biomineralization and the ubiquitylation processes.Dong FangCong PanHuijuan LinYa LinGuangrui XuGuiyou ZhangHongzhong WangLiping XieRongqing ZhangPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 4, p e35715 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Dong Fang Cong Pan Huijuan Lin Ya Lin Guangrui Xu Guiyou Zhang Hongzhong Wang Liping Xie Rongqing Zhang Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix.
description	Mollusks shell formation is mediated by matrix proteins and many of these proteins have been identified and characterized. However, the mechanisms of protein control remain unknown. Here, we report the ubiquitylation of matrix proteins in the prismatic layer of the pearl oyster, Pinctada fucata. The presence of ubiquitylated proteins in the prismatic layer of the shell was detected with a combination of western blot and immunogold assays. The coupled ubiquitins were separated and identified by Edman degradation and liquid chromatography/mass spectrometry (LC/MS). Antibody injection in vivo resulted in large amounts of calcium carbonate randomly accumulating on the surface of the nacreous layer. These ubiquitylated proteins could bind to specific faces of calcite and aragonite, which are the two main mineral components of the shell. In the in vitro calcium carbonate crystallization assay, they could reduce the rate of calcium carbonate precipitation and induce the calcite formation. Furthermore, when the attached ubiquitins were removed, the functions of the EDTA-soluble matrix of the prismatic layer were changed. Their potency to inhibit precipitation of calcium carbonate was decreased and their influence on the morphology of calcium carbonate crystals was changed. Taken together, ubiquitylation is involved in shell formation. Although the ubiquitylation is supposed to be involved in every aspect of biophysical processes, our work connected the biomineralization-related proteins and the ubiquitylation mechanism in the extracellular matrix for the first time. This would promote our understanding of the shell biomineralization and the ubiquitylation processes.
format	article
author	Dong Fang Cong Pan Huijuan Lin Ya Lin Guangrui Xu Guiyou Zhang Hongzhong Wang Liping Xie Rongqing Zhang
author_facet	Dong Fang Cong Pan Huijuan Lin Ya Lin Guangrui Xu Guiyou Zhang Hongzhong Wang Liping Xie Rongqing Zhang
author_sort	Dong Fang
title	Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix.
title_short	Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix.
title_full	Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix.
title_fullStr	Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix.
title_full_unstemmed	Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix.
title_sort	ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/b53787dcd35d4de39d29e8c0f2fc2f2a
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Ubiquitylation functions in the calcium carbonate biomineralization in the extracellular matrix.

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