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characterization of an unusual tropoelastin with truncated C-terminus in the frog.

Characterization of an unusual tropoelastin with truncated C-terminus in the frog.

机构信息

Molecular Structure and Function Program, Hospital for Sick Children, Toronto, Canada.

出版信息

Matrix Biol. 2009 Sep;28(7):432-41. doi: 10.1016/j.matbio.2009.07.003. Epub 2009 Jul 26.

DOI:10.1016/j.matbio.2009.07.003
PMID:19638308
Abstract

Tropoelastin is the monomeric form of elastin, a major polymeric protein of the extracellular elastic matrix of vertebrate tissues with properties of extensibility and elastic recoil. Mammalian and avian species contain a single gene for tropoelastin. A tropoelastin gene has also previously been identified in amphibians. In contrast, two tropoelastin genes with different tissue expression patterns have been described in teleosts. While general characteristics of tropoelastins, such as alternating arrangements of hydrophobic and crosslinking domains, are conserved across a wide phylogenetic range, sequences of these domains are highly variable, particularly when amphibian and teleost tropoelastins are included. For this reason exon-to-exon correspondence is not clear, and overall alignment of tropoelastin sequences across all species is not possible. An exception to this is the C-terminal exon, whose coding sequence has been very well-conserved across all species described to date. In mammalians this C-terminal domain has been shown to be important for interactions with cells and other matrix-associated proteins involved in matrix assembly. Here we identify and characterize a second tropoelastin gene in the frog with several unusual characteristics, the most striking of which is truncation of the C-terminal domain, deleting normally conserved sequence motifs. We demonstrate that, in spite of the absence of these motifs, both frog tropoelastin genes are expressed and incorporated into the elastic matrix, although with differential tissue localizations.

摘要

原肌球蛋白是弹性蛋白的单体形式,是脊椎动物组织细胞外弹性基质的主要聚合蛋白,具有伸展性和弹性回弹的特性。哺乳动物和鸟类都含有一个原肌球蛋白基因。以前在两栖动物中也发现了一个原肌球蛋白基因。相比之下,在硬骨鱼中已经描述了两个具有不同组织表达模式的原肌球蛋白基因。虽然原肌球蛋白的一般特征,如疏水性和交联结构域的交替排列,在广泛的系统发育范围内是保守的,但这些结构域的序列高度可变,特别是当包括两栖动物和硬骨鱼的原肌球蛋白时。因此,外显子-外显子的对应关系并不清楚,也不可能对所有物种的原肌球蛋白序列进行整体比对。一个例外是 C 末端外显子,其编码序列在迄今为止描述的所有物种中都得到了很好的保守。在哺乳动物中,这个 C 末端结构域已被证明对与细胞的相互作用以及参与基质组装的其他基质相关蛋白很重要。在这里,我们在青蛙中鉴定并表征了第二个具有几个不寻常特征的原肌球蛋白基因,其中最显著的是 C 末端结构域的截断,删除了通常保守的序列基序。我们证明,尽管缺乏这些基序,但两个青蛙原肌球蛋白基因都表达并整合到弹性基质中,尽管组织定位不同。

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Characterization of an unusual tropoelastin with truncated C-terminus in the frog. characterization of an unusual tropoelastin with truncated C-terminus in the frog.
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Heparan sulphate interacts with tropoelastin, with some tropoelastin peptides and is present in human dermis elastic fibers.硫酸乙酰肝素与原弹性蛋白、一些原弹性蛋白肽相互作用,并存在于人类真皮弹性纤维中。
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引用本文的文献

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Tropoelastin and Elastin Assembly.原弹性蛋白与弹性蛋白组装
Front Bioeng Biotechnol. 2021 Feb 25;9:643110. doi: 10.3389/fbioe.2021.643110. eCollection 2021.
2
Elastin is heterogeneously cross-linked.弹性蛋白呈异质交联。
J Biol Chem. 2018 Sep 28;293(39):15107-15119. doi: 10.1074/jbc.RA118.004322. Epub 2018 Aug 14.
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Modelling the self-assembly of elastomeric proteins provides insights into the evolution of their domain architectures.模拟弹性蛋白的自组装为研究其结构域架构的演化提供了深入的了解。
PLoS Comput Biol. 2012;8(3):e1002406. doi: 10.1371/journal.pcbi.1002406. Epub 2012 Mar 1.