Conservation of intrinsic disorder in protein domains and families: II. Functions of conserved disorder
Conservation of intrinsic disorder in protein domains and families: II. Functions of conserved disorder
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DOI：
10.1021/pr060049p
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发表时间：
2006-04-01
影响因子：
4.4
通讯作者：
Dunker, AK
中科院分区：
文献类型：
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作者：
Chen, JW;Romero, P;Dunker, AK
保守性疾病预测（CDP）的区域被发现在蛋白质结构域从所有可用的InterPro成员数据库，虽然有不同的频率。这些CDP区域存在于所有生命王国的蛋白质中，包括病毒。然而，真核生物比古细菌和细菌多1个数量级的蛋白质含有长无序区域。CDP区域的序列保守性各不相同，但平均略低于保守顺序的区域。在某些情况下，无序区域比有序区域演化得更快，在其他情况下它们演化得更慢，而在其他情况下它们以大致相同的速率演化。发现多种功能与含有保守性紊乱的结构域相关。最常见的是DNA/RNA结合和蛋白质结合。许多核糖体蛋白也被发现含有保守的无序区域。其他功能包括膜转位和氨基酸储存发芽。由于目前知识的局限性以及这项工作所使用的方法，无法确定这些功能是否与预测的无序区域直接相关。然而，这项工作中与保守无序相关的功能与其他研究中发现的与无序区域相关的功能一致。我们已经确定，细菌和古细菌蛋白质中的内在紊乱可能比以前认为的更常见，但这种紊乱可能用于与真核蛋白质不同的目的，以及发生在较短的蛋白质片段中。预测的疾病区域被发现是保守的大量的蛋白质家族和结构域。虽然许多人认为这些保守的结构域是有序的，但事实上，它们中的相当数量包含可能对其功能至关重要的无序区域。
Regions of conserved disorder prediction (CDP) were found in protein domains from all available InterPro member databases, although with varying frequency. These CDP regions were found in proteins from all kingdoms of life, including viruses. However, eukaryotes had 1 order of magnitude more proteins containing long disordered regions than did archaea and bacteria. Sequence conservation in CDP regions varied, but was on average slightly lower than in regions of conserved order. In some cases, disordered regions evolve faster than ordered regions, in others they evolve slower, and in the rest they evolve at roughly the same rate. A variety of functions were found to be associated with domains containing conserved disorder. The most common were DNA/RNA binding, and protein binding. Many ribosomal proteins also were found to contain conserved disordered regions. Other functions identified included membrane translocation and amino acid storage for germination. Due to limitations of current knowledge as well as the methodology used for this work, it was not determined whether these functions were directly associated with the predicted disordered region. However, the functions associated with conserved disorder in this work are in agreement with the functions found in other studies to correlate to disordered regions. We have established that intrinsic disorder may be more common in bacterial and archaeal proteins than previously thought, but this disorder is likely to be used for different purposes than in eukaryotic proteins, as well as occurring in shorter stretches of protein. Regions of predicted disorder were found to be conserved within a large number of protein families and domains. Although many think of such conserved domains as being ordered, in fact a significant number of them contain regions of disorder that are likely to be crucial to their functions.