Review: Post-translational modifications of marine shell matrix proteins

被引：8

作者：

Rivera-Perez, Crisalejandra ^{[1
]}

Hernandez-Saavedra, Norma Y. ^{[2
]}

机构：

[1] CONACYT, Ctr Invest Biol Noroeste CIBNOR, La Paz, Baja California, Mexico

[2] Ctr Invest Biol Noroeste CIBNOR, Mol Genet Lab, La Paz 23096, Baja California, Mexico

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 2021年 / 256卷

关键词：

SMPs; PTMs; Biomineralization; Glycosylation; Phosphorylation; EXTRAPALLIAL FLUID PROTEIN; HALIOTIS-LAEVIGATA NACRE; PEARL OYSTER; ORGANIC MATRIX; BIOMINERALIZATION PROTEINS; MOLECULAR-MECHANISM; PROTEOMIC ANALYSIS; PRISMATIC LAYER; BINDING PROTEIN; ACIDIC PROTEINS;

D O I：

10.1016/j.cbpb.2021.110641

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Shell matrix proteins (SMPs) are key components for the Mollusk shell biomineralization. SMPs function has been hypothesized in several proteins by bioinformatics analysis, and through in vitro crystallization assays. However, studies of the post-translational modifications (PTMs) of SMPs, which contribute to their structure and the function, are limited. This review provides the current status of the SMPs with the most common PTMs described (glycosylation, phosphorylation, and disulfide bond formation) and their role in shell biomineralization. Also, recent studies based on recombinant production of SMPs are discussed. Finally, recommendations for the study of SMPs and their PTMs are provided. The review showed that PTMs are widely distributed in SMPs, and their presence on SMPs may contribute to the modulation of their activity in some SMPs, contributing to the crystal growth formation and differentiation through different mechanisms, however, in a few cases the lack of the PTMs do not alter their inherent function.

引用

页数：10

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