F-box-like domains are present in most poxvirus ankyrin repeat proteins
F-box-like domains are present in most poxvirus ankyrin repeat proteins
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DOI：
10.1007/s11262-005-1784-z
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发表时间：
2005-10-01
期刊：
影响因子：
1.6
通讯作者：
Ueda, N
中科院分区：
文献类型：
--
作者：
Mercer, AA;Fleming, SB;Ueda, N
脊椎动物痘病毒编码大量带有Ank重复序列的蛋白质，蛋白质之间相互作用，但对这个大家族的作用(S)知之甚少。我们在这里报道，绝大多数痘病毒ANK重复蛋白都有一个通用的分子结构，在羧基末端包含一个保守的氨基酸基序。这个基序最像是在一系列细胞蛋白中看到的F-box。从任何一种痘病毒的ANK重复蛋白中，80%-100%具有F-box样结构域，我们只观察到一种具有F-box样结构域的痘病毒蛋白，但缺乏ANK重复。只有一种脊椎动物痘病毒的蛋白缺乏F-box样结构域，该属不编码ANK重复蛋白。许多F-box蛋白是泛素连接酶复合体的识别亚单位，其中F-box与复合体的核心元件结合，其余蛋白质相互作用区域与底物蛋白结合。这些观察结果提出了痘病毒ANK-F-box蛋白功能的一般模型。我们认为，这些蛋白质中的F-box-like结构域与细胞泛素连接酶复合体相互作用，从而指导与ANK重复序列结合的蛋白质的泛素化。大量不同的痘病毒ANK-F-box蛋白表明，广泛的细胞蛋白可能受到泛素介导的降解，从而调节不同的细胞对病毒感染的反应。
Vertebrate poxviruses encode numerous proteins with the ankyrin (ANK) repeat, protein-protein interaction motif but little is known about the role(s) of this large family of poxvirus proteins. We report here that the vast majority of poxvirus ANK repeat proteins share a general molecular architecture that includes a conserved amino acid motif at the carboxyl terminus. This motif is most like the F-box seen in a range of cellular proteins. From 80-100% of the ANK repeat proteins of any one poxvirus have an F-box-like domain and we observed only one poxvirus protein with an F-box-like domain but lacking ANK repeats. The proteins of only one genus of vertebrate poxviruses lack F-box-like domains and this genus does not encode ANK repeat proteins. Many F-box proteins are recognition subunits of ubiquitin ligase complexes in which the F-box binds to core elements of the complex and protein-protein interaction domains in the remainder of the protein bind the substrate protein. These observations suggest a general model of the function of the poxvirus ANK-F-box proteins. We propose that the F-box-like domains in these proteins interact with cellular ubiquitin ligase complexes and thereby direct the ubiquitination of proteins bound to the ANK repeats. The large number of different poxviral ANK-F-box proteins suggests a wide range of cellular proteins might be subjected to ubiquitin-mediated degradation, thereby modulating diverse cellular responses to viral infection.