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The UBE2E proteins as conjugating dispersers: Extending function with extended extensions

机译：UBE2E蛋白作为共轭分散剂：扩展功能，扩展功能

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In this issue of the Journal of Molecular Biology, Schumacher et al. investigate the molecular mechanisms underlying the ability of the members of Class II ubiquitin-conjugating enzymes (E2s) to catalyze the formation of polyubiquitin chains [1]. In addition to the highly conserved catalytic domain (the core ubiquitin-conjugating domain, UBC, of -150 residues), the human UBE2E proteins studied here contain N-terminal intrinsically disordered (ID) extensions of different lengths [2]. The authors suggest that these extended extensions are a key for extending the E2 functionality. The impact of this important observation goes far beyond the understanding of how the ubiquitination machinery acts, since (a) it argues that studying the intact proteins, not just their core catalytic domains, is important for complete understanding of protein functionality, and (b) it provides new clues on how the protein functionality can be controlled and modulated via non-catalytic and therefore seemingly useless extended extensions, ID regions. A brief description of what is extended (i.e., a short description of the protein intrinsic disorder phenomenon with the focus on disordered tails) from what (i.e., an overview of the ubiquitination machinery with the focus on UBE2E proteins) is given below to help better appreciate the importance of these conclusions.
机译：在本期《分子生物学杂志》上，舒马赫等人。研究了II类泛素结合酶（E2s）成员催化多聚泛素链形成的能力的分子机制[1]。除了高度保守的催化结构域（-150个残基的核心泛素结合结构域UBC）之外，本文研究的人UBE2E蛋白还包含不同长度的N端固有无序（ID）延伸[2]。作者认为，这些扩展的扩展是扩展E2功能的关键。这项重要观察的影响远远超出了对泛素化机制的理解，因为（a）认为研究完整的蛋白质，而不仅仅是其核心催化结构域，对于全面理解蛋白质功能至关重要，并且（b）它提供了有关如何通过非催化的，因此似乎无用的扩展延伸区，ID区来控制和调节蛋白质功能的新线索。为了更好的帮助，下面给出了扩展内容的简要说明（即，以尾巴无序为重点的蛋白质固有紊乱现象的简短描述）（以UBE2E蛋白为重点的泛素化机制的概述），以帮助更好地进行分析。赞赏这些结论的重要性。

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