Regulation of protein function by interfering protein species.
Regulation of protein function by interfering protein species.
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DOI：
10.1515/bmc.2011.053
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发表时间：
2012-02-01
影响因子：
--
通讯作者：
Wenkel, Stephan
中科院分区：
文献类型：
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作者：
Graeff, Moritz;Wenkel, Stephan
摘要大多数蛋白质不是单独起作用，而是以蛋白质复合体的形式起作用。对于几种转录调节因子，已知它们在DNA结合之前必须同源二聚化或异源二聚化。这些蛋白质相互作用通过定义的蛋白质-蛋白质相互作用（PPI）结构域发生。二十多年前，DNA结合抑制剂（inhibitor of DNA binding，ID），一种含有单个螺旋-环-螺旋（helix-loop-helix，HLH）基序的小蛋白被鉴定出来。ID能够与较大的DNA结合碱性螺旋-环-螺旋（bHLH）转录因子相互作用，但由于缺乏DNA结合所需的碱性结构域，ID将bHLH蛋白捕获在非功能性复合物中。在植物中的工作，在最近几年中，确定了更多的小蛋白类似ID。这些小的负作用蛋白的一个标志是存在的蛋白质相互作用域和转录激活或DNA结合所需的其他功能域的情况下。由于这些蛋白质通常非常小，并且类似于microRNA（意思是以显性负性方式）起作用，因此我们建议将这些蛋白质种类称为“microProteins”（miPs）。miPs可以在基因组中编码为单独的转录单位，但也可以通过选择性剪接产生。其他负作用的蛋白质，由一个以上的结构域组成，也已被确定，我们建议将这些蛋白质称为“干扰蛋白”（iPs）。本文的目的是更准确地说明如何区分miPs从iPs。因此，我们将重点介绍这两种蛋白质种类的最新发现，并描述它们的作用模式。此外，miPs具有调节不同功能的蛋白质的能力，强调了它们作为生物技术工具的价值。
Abstract Most proteins do not function alone but act in protein complexes. For several transcriptional regulators, it is known that they have to homo- or heterodimerize prior to DNA binding. These protein interactions occur through defined protein-protein-interaction (PPI) domains. More than two decades ago, inhibitor of DNA binding (ID), a small protein containing a single helix-loop-helix (HLH) motif was identified. ID is able to interact with the larger DNA-binding basic helix-loop-helix (bHLH) transcription factors, but due to the lack of the basic domain required for DNA binding, ID traps bHLH proteins in non-functional complexes. Work in plants has, in the recent years, identified more small proteins acting in analogy to ID. A hallmark of these small negative acting proteins is the presence of a protein-interaction domain and the absence of other functional domains required for transcriptional activation or DNA binding. Because these proteins are often very small and function in analogy to microRNAs (meaning in a dominant-negative manner), we propose to refer to these protein species as 'microProteins' (miPs). miPs can be encoded in the genome as individual transcription units but can also be produced by alternative splicing. Other negatively acting proteins, consisting of more than one domain, have also been identified, and we propose to call these proteins 'interfering proteins' (iPs). The aim of this review is to state more precisely how to discriminate miPs from iPs. Therefore, we will highlight recent findings on both protein species and describe their mode of action. Furthermore, miPs have the ability to regulate proteins of diverse functions, emphasizing their value as biotechnological tools.