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首页> 外文期刊>Journal of Molecular Biology >An Ancient Autoproteolytic Domain Found in GAIN, ZU5 and Nucleoporin98
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An Ancient Autoproteolytic Domain Found in GAIN, ZU5 and Nucleoporin98

机译：在GAIN，ZU5和Nucleoporin98中发现的一个古老的自蛋白水解域

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A large family of G protein-coupled receptors (GPCRs) involved in cell adhesion has a characteristic autoproteolysis motif of HLT/S known as the GPCR proteolysis site (GPS). GPS is also shared by polycystic kidney disease proteins and it precedes the first transmembrane segment in both families. Recent structural studies have elucidated the GPS to be part of a larger domain named GPCR autoproteolysis inducing (GAIN) domain. Here we demonstrate the remote homology relationships of GAIN domain to ZU5 domain and Nucleoporin98 (Nup98) C-terminal domain by structural and sequence analysis. Sequence homology searches were performed to extend ZU5-like domains to bacteria and archaea, as well as new eukaryotic families. We found that the consecutive ZU5-UPA-death domain domain organization is commonly used in human cytoplasmic proteins with ZU5 domains, including CARD8 (caspase recruitment domain-containing protein 8) and NLRP1 (NACHT, LRR and PYD domain-containing protein 1) from the FIIND (Function to Find) family. Another divergent family of extracellular ZU5-like domains was identified in cartilage intermediate layer proteins and FAM171 proteins. Current diverse families of GAIN domain subdomain B, ZU5 and Nup98 C-terminal domain likely evolved from an ancient autoproteolytic domain with an HFS motif. The autoproteolytic site was kept intact in Nup98, p53-induced protein with a death domain and UNC5C-like, deteriorated in many ZU5 domains and changed in GAIN and FIIND. Deletion of the strand after the cleavage site was observed in zonula occluden-1 and some Nup98 homologs. These findings link several autoproteolytic domains, extend our understanding of GAIN domain origination in adhesion GPCRs and provide insights into the evolution of an ancient autoproteolytic domain. (C) 2014 Elsevier Ltd. All rights reserved.
机译：参与细胞粘附的大量G蛋白偶联受体（GPCR）具有HLT / S的特征性自蛋白水解基序，称为GPCR蛋白水解位点（GPS）。 GPS还与多囊肾疾病蛋白共享，并且在两个家族的第一个跨膜片段之前。最近的结构研究已阐明GPS是名为GPCR自蛋白水解诱导（GAIN）域的较大域的一部分。在这里，我们通过结构和序列分析证明了GAIN结构域与ZU5结构域和Nucleoporin98（Nup98）C末端结构域的远程同源关系。进行序列同源性搜索以将ZU5样结构域扩展到细菌和古细菌以及新的真核生物家族。我们发现连续的ZU5-UPA-死亡域结构域组织通常用于具有ZU5域的人胞质蛋白，包括CARD8（含胱天蛋白酶募集结构域蛋白8）和NLRP1（NACHT，LRR和PYD结构域蛋白1）。 FIIND（查找功能）系列。在软骨中间层蛋白和FAM171蛋白中鉴定出另一个不同的细胞外ZU5类结构域家族。当前的GAIN域亚域B，ZU5和Nup98 C末端域的不同家族可能是从具有HFS主题的古老自蛋白水解域演变而来的。自动蛋白水解位点在Nup98，p53诱导的具有死亡结构域和UNC5C样的蛋白中保持完整，在许多ZU5结构域中变质并在GAIN和FIIND中发生改变。在卵裂小带-1和一些Nup98同源物中观察到切割位点后链的缺失。这些发现链接了几个自蛋白水解结构域，扩展了我们对粘附GPCR中GAIN域起源的理解，并提供了对古老自蛋白结构域进化的见解。 （C）2014 Elsevier Ltd.保留所有权利。

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