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从cDNA数据推断灵长类动物中zonadhesin D结构域的序列进化、加工及翻译后修饰

Sequence evolution, processing, and posttranslational modification of zonadhesin D domains in primates, as inferred from cDNA data.

作者信息

Herlyn Holger, Zischler Hans

机构信息

Institute of Anthropology, University of Mainz, Colonel-Kleinmann-Weg 2 (SB II), D-55099 Mainz, Germany.

出版信息

Gene. 2005 Dec 5;362:85-97. doi: 10.1016/j.gene.2005.06.009. Epub 2005 Sep 26.

Abstract

Zonadhesin is a mammalian transmembrane sperm ligand. Precursor zonadhesin essentially consists of MAM (meprin/A5 antigen/mu receptor tyrosine phosphatase) domains, a mucin-like repeat, and D domains (homologous to von Willebrand D). Recent immunovisualization and binding assays indicate that zonadhesin D domains 1-3 bind postacrosomally to the zona pellucida. This feature has attracted considerable interest in the evolution of zonadhesin and its possible biological and biomedical implications. Previous molecular evolutionary analyses, however, were confined to cDNA sequences of only few distantly related species. Moreover, except for rabbit and pig, little is known about zonadhesin's processing. To delineate the situation in primates including humans, we analyze here the evolution of zonadhesin on the basis of D domain encoding cDNAs of about 4900 base pairs (bp) length from a representative primate sampling (1 Strepsirhini, 3 Cercopithecidae, 3 Platyrrhini, and human; 7 new sequences) plus GenBank data from mouse, rabbit, and pig. Site-specific (CODEML and HyPhy) analysis indicates positive evolution of zonadhesin. Moreover, moving window analysis (CRANN) points to a positive correlation of sequence evolution and sperm-competition. Significant accumulations of positively selected sites across interspecifically variable motifs (identified by PROSITE) suggest that positive selection promotes differences between species by amino acid exchanges and changes in posttranslational modification. In the case of zonadhesin D domains, positive selection might thus contribute to the species-specific binding of zonadhesin and zona pellucida. A high conservation of processing and dimerization motifs of primate zonadhesin in analogy to pig, on the other hand, illustrates that zonadhesin's backbone needs to meet basic requirements in order to retain function.

摘要

透明带黏附素是一种哺乳动物跨膜精子配体。前体透明带黏附素主要由MAM(膜金属蛋白酶/载脂蛋白A5抗原/μ受体酪氨酸磷酸酶)结构域、一个黏蛋白样重复序列和D结构域(与血管性血友病因子D结构域同源)组成。最近的免疫可视化和结合试验表明,透明带黏附素的D结构域1 - 3在顶体后与透明带结合。这一特性引起了人们对透明带黏附素进化及其可能的生物学和生物医学意义的极大兴趣。然而,以往的分子进化分析仅限于少数远缘物种的cDNA序列。此外,除了兔子和猪,人们对透明带黏附素的加工过程知之甚少。为了阐明包括人类在内的灵长类动物的情况,我们在此基于约4900个碱基对(bp)长度的D结构域编码cDNA,对来自代表性灵长类样本(1种原猴亚目、3种猕猴科、3种阔鼻猴亚目和人类;7个新序列)以及来自小鼠、兔子和猪的GenBank数据,分析透明带黏附素的进化。位点特异性分析(CODEML和HyPhy)表明透明带黏附素存在正向进化。此外,移动窗口分析(CRANN)表明序列进化与精子竞争呈正相关。在种间可变基序(由PROSITE鉴定)中,正选择位点的显著积累表明,正选择通过氨基酸交换和翻译后修饰的变化促进了物种间的差异。因此,就透明带黏附素D结构域而言,正选择可能有助于透明带黏附素与透明带的物种特异性结合。另一方面,与猪类似,灵长类动物透明带黏附素的加工和二聚化基序高度保守,这说明透明带黏附素的主干需要满足基本要求才能保持功能。

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