Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins.
Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins.
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DOI：
10.1093/nar/gkj424
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发表时间：
2006
影响因子：
14.9
通讯作者：
Iakoucheva LM
中科院分区：
文献类型：
--
作者：
Haynes C;Iakoucheva LM
富含丝氨酸/精氨酸的剪接因子在结构性剪接和选择性剪接以及RNA代谢的几个步骤中发挥着重要作用。尽管迄今为止积累了大量关于SR蛋白的功能信息，但关于该家族成员的结构知识非常有限。为了更好地了解SR蛋白的结构-功能关系，我们对SR蛋白家族成员进行了广泛的序列分析，并将其与有序/无序结构预测相结合。我们发现SR蛋白具有固有无序(ID)蛋白的特性。SR蛋白的氨基酸组成和序列复杂性与无序蛋白质区非常相似。更详细的分析表明，与整个人类蛋白质组相比，SR蛋白，特别是其RS结构域，富含促进无序的残基，而缺乏促进有序的残基。此外，无序预测表明，SR蛋白的RS结构域是完全非结构化的。两种不同的分类方法，电荷疏水度和无序分数的累积分布函数(CDF)是一致的，它们都强烈预测了SR蛋白家族的成员是无序的。这项研究强调了无序结构对SR蛋白的几个功能的重要性，如剪接体组装和与多个伙伴的相互作用。此外，它还证明了有序/无序预测对于从序列中推断蛋白质结构的有效性。
Serine/arginine-rich (SR) splicing factors play an important role in constitutive and alternative splicing as well as during several steps of RNA metabolism. Despite the wealth of functional information about SR proteins accumulated to-date, structural knowledge about the members of this family is very limited. To gain a better insight into structure-function relationships of SR proteins, we performed extensive sequence analysis of SR protein family members and combined it with ordered/disordered structure predictions. We found that SR proteins have properties characteristic of intrinsically disordered (ID) proteins. The amino acid composition and sequence complexity of SR proteins were very similar to those of the disordered protein regions. More detailed analysis showed that the SR proteins, and their RS domains in particular, are enriched in the disorder-promoting residues and are depleted in the order-promoting residues as compared to the entire human proteome. Moreover, disorder predictions indicated that RS domains of SR proteins were completely unstructured. Two different classification methods, the charge-hydropathy measure and the cumulative distribution function (CDF) of the disorder scores, were in agreement with each other, and they both strongly predicted members of the SR protein family to be disordered. This study emphasizes the importance of the disordered structure for several functions of SR proteins, such as for spliceosome assembly and for interaction with multiple partners. In addition, it demonstrates the usefulness of order/disorder predictions for inferring protein structure from sequence.
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影响因子：
2.9
作者：
Dunker, AK;Lawson, JD;Obradovic, Z
通讯作者：
Obradovic, Z
影响因子：
4.8
作者：
Konrat, R;Kräutler, B;Bister, K
通讯作者：
Bister, K
DOI：
10.1073/pnas.181354098
发表时间：
2001-08-28
影响因子：
11.1
作者：
Lai, MC;Lin, RI;Tarn, WY
通讯作者：
Tarn, WY
影响因子：
14.9
作者：
Bairoch, A;Apweiler, R
通讯作者：
Apweiler, R
影响因子：
64.5
作者：
Kielkopf, CL;Rodionova, NA;Burley, SK
通讯作者：
Burley, SK