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首页> 外文期刊>Journal of Molecular Biology >Extensive and modular intrinsically disordered segments in C. elegans TTN-1 and implications in filament binding, elasticity and oblique striation.
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Extensive and modular intrinsically disordered segments in C. elegans TTN-1 and implications in filament binding, elasticity and oblique striation.

机译：秀丽隐杆线虫TTN-1中广泛和模块化的内在无序节段及其对细丝结合，弹性和斜纹的影响。

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TTN-1, a titin like protein in Caenorhabditis elegans, is encoded by a single gene and consists of multiple Ig and fibronectin 3 domains, a protein kinase domain and several regions containing tandem short repeat sequences. We have characterized TTN-1's sarcomere distribution, protein interaction with key myofibrillar proteins as well as the conformation malleability of representative motifs of five classes of short repeats. We report that two antibodies developed to portions of TTN-1 detect an approximately 2-MDa polypeptide on Western blots. In addition, by immunofluorescence staining, both of these antibodies localize to the I-band and may extend into the outer edge of the A-band in the obliquely striated muscle of the nematode. Six different 300-residue segments of TTN-1 were shown to variously interact with actin and/or myosin in vitro. Conformations of synthetic peptides of representative copies of each of the five classes of repeats--39-mer PEVT, 51-mer CEEEI, 42-mer AAPLE, 32-mer BLUE and 30-mer DispRep--were investigated by circular dichroism at different temperatures, ionic strengths and solvent polarities. The PEVT, CEEEI, DispRep and AAPLE peptides display a combination of a polyproline II helix and an unordered structure in aqueous solution and convert in trifluoroethanol to alpha-helix (PEVT, CEEEI, DispRep) and beta-turn (AAPLE) structures, respectively. The octads in BLUE motifs form unstable alpha-helix-like structures coils in aqueous solution and negligible heptad-based, alpha-helical coiled-coils. The alpha-helical structure, as modeled by threading and molecular dynamics simulations, tends to form helical bundles and crosses based on its 8-4-2-2 hydrophobic helical patterns and charge arrays on its surface. Our finding indicates that APPLE, PEVT, CEEEI and DispRep regions are all intrinsically disordered and highly reminiscent of the conformational malleability and elasticity of vertebrate titin PEVK segments. The proposed presence of long, modular and unstable alpha-helical oligomerization domains in the BLUE region of TTN-1 could bundle TTN-1 and stabilize oblique striation of the sarcomere.
机译：TTN-1是秀丽隐杆线虫中的类似肌钙蛋白的蛋白，由单个基因编码，由多个Ig和纤连蛋白3结构域，一个蛋白激酶结构域以及几个包含串联短重复序列的区域组成。我们已经表征了TTN-1的肌节分布，与关键肌原纤维蛋白的蛋白相互作用以及五类短重复的代表性基序的构象可塑性。我们报告说，两种针对TTN-1部分发展的抗体在Western印迹上检测到大约2-MDa多肽。此外，通过免疫荧光染色，这两种抗体均位于I波段，并可能延伸到线虫斜纹肌中A波段的外边缘。 TTN-1的六个不同的300个残基片段显示在体外与肌动蛋白和/或肌球蛋白发生各种相互作用。通过不同的圆二色性研究五种重复类型的代表肽的合成肽的构象-39-mer PEVT，51-mer CEEEI，42-mer AAPLE，32-mer BLUE和30-mer DispRep温度，离子强度和溶剂极性。 PEVT，CEEEI，DispRep和AAPLE肽在水溶液中显示出聚脯氨酸II螺旋和无序结构的组合，并在三氟乙醇中分别转化为α-螺旋（PEVT，CEEEI，DispRep）和β-转角（AAPLE）结构。 BLUE图案中的八位字母在水溶液中形成不稳定的α-螺旋状结构线圈，而基于庚烷的可忽略的α-螺旋线圈状线圈则微不足道。通过穿线和分子动力学模拟建模的α-螺旋结构，倾向于基于其表面上的8-4-2-2疏水螺旋图形和电荷阵列形成螺旋束和交叉。我们的发现表明，APPLE，PEVT，CEEEI和DispRep区域都是内在无序的，并且高度让人联想到脊椎动物titin PEVK段的构象可塑性和弹性。建议在TTN-1的BLUE区域中存在长的，模块化且不稳定的α-螺旋低聚域，这可能会束缚TTN-1并稳定肌节的斜纹。

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