Molecular evolution of type VI intermediate filament proteins.
Molecular evolution of type VI intermediate filament proteins.
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DOI：
10.1186/1471-2148-7-164
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发表时间：
2007-09-13
影响因子：
3.4
通讯作者：
Vincent M
中科院分区：
文献类型：
--
作者：
Guérette D;Khan PA;Savard PE;Vincent M
Tanabin、transitin和nestin分别是蛙类、鸟类和哺乳动物中受发育调控的VI型中间丝蛋白。Tanabin在胚胎脊椎动物神经元的生长锥中表达，而transtin和nestin则在肌源性和神经源性细胞中表达。另一种VI型IF蛋白，synemin，在鸟类和哺乳动物的未分化和成熟肌肉细胞中表达。除了IF典型的α-螺旋核心结构域外，VI型IF蛋白的特征是一个长c端尾部，通常包含不同的重复基序。VI型IF蛋白的分子进化研究仍然很少。为了研究VI型IF蛋白的进化史，进行了序列比较、BLAST搜索、synsyn研究和系统发育分析。本研究提供了新的证据，证明tanabin、transitin和nestin确实是同源的VI型IF蛋白。结果表明，tanabin， transitin和nestin基因共享内含子位置和序列特征，具有相似的染色体背景，并且在系统发育分析中显示出密切相关的位置。尽管具有这种同源性，但它们的c端末端的快速进化速度导致了具有不同生物活性的重复基序的出现。特别是，我们对它们尾部结构域的计算机和体外分析表明（鸟类）过渡蛋白，而不是（哺乳动物）巢蛋白，包含一个显示核苷酸水解活性的重复结构域。这些对IF蛋白进化史的分析符合一个模型，在这个模型中，VI型IF形成一个与NF蛋白不同的分支，由两种主要蛋白组成：synemin和nestin同源物。巢蛋白同源物c末端的快速进化可能是其功能分化的原因。
Tanabin, transitin and nestin are type VI intermediate filament (IF) proteins that are developmentally regulated in frogs, birds and mammals, respectively. Tanabin is expressed in the growth cones of embryonic vertebrate neurons, whereas transitin and nestin are found in myogenic and neurogenic cells. Another type VI IF protein, synemin, is expressed in undifferentiated and mature muscle cells of birds and mammals. In addition to an IF-typical α-helical core domain, type VI IF proteins are characterized by a long C-terminal tail often containing distinct repeated motifs. The molecular evolution of type VI IF proteins remains poorly studied. To examine the evolutionary history of type VI IF proteins, sequence comparisons, BLAST searches, synteny studies and phylogenic analyses were performed. This study provides new evidence that tanabin, transitin and nestin are indeed orthologous type VI IF proteins. It demonstrates that tanabin, transitin and nestin genes share intron positions and sequence identities, have a similar chromosomal context and display closely related positions in phylogenic analyses. Despite this homology, fast evolution rates of their C-terminal extremity have caused the appearance of repeated motifs with distinct biological activities. In particular, our in silico and in vitro analyses of their tail domain have shown that (avian) transitin, but not (mammalian) nestin, contains a repeat domain displaying nucleotide hydrolysis activity. These analyses of the evolutionary history of the IF proteins fit with a model in which type VI IFs form a branch distinct from NF proteins and are composed of two major proteins: synemin and nestin orthologs. Rapid evolution of the C-terminal extremity of nestin orthologs could be responsible for their divergent functions.
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影响因子：
7.5
作者：
Herrmann, H;Aebi, U
通讯作者：
Aebi, U
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2.5
作者：
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LEWIS, SA;COWAN, NJ
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作者：
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作者：
GRANGER, BL;LAZARIDES, E
通讯作者：
LAZARIDES, E