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The more the merrier: how homo-oligomerization alters the interactome and function of ribonucleotide reductase.
Current Opinion in Chemical Biology ( IF 6.9 ) Pub Date : 2019-11-15 , DOI: 10.1016/j.cbpa.2019.09.003
Marcus J C Long 1 , Alexandra Van Hall-Beauvais 2 , Yimon Aye 2
Affiliation  

Stereotyped as a nexus of dNTP synthesis, the dual-subunit enzyme - ribonucleotide reductase (RNR) - is coming into view as a paradigm of oligomerization and moonlighting behavior. In the present issue of 'omics', we discuss what makes the larger subunit of this enzyme (RNR-α) so interesting, highlighting its emerging cellular interactome based on its unique oligomeric dynamism that dictates its compartment-specific occupations. Linking the history of the field with the multivariable nature of this exceedingly sophisticated enzyme, we further discuss implications of new data pertaining to DNA-damage response, S-phase checkpoints, and ultimately tumor suppression. We hereby hope to provide ideas for those interested in these fields and exemplify conceptual frameworks and tools that are useful to study RNR's broader roles in biology.

中文翻译:

越多越好:均聚如何改变核糖核苷酸还原酶的相互作用组和功能。

刻板印象是dNTP合成的联系,双亚基酶-核糖核苷酸还原酶(RNR)-被视为低聚和月光照行为的范例。在本期《组学》中,我们讨论了使这种酶的更大亚基(RNR-α)如此有趣的原因,并突出了其新兴的细胞相互作用基因组,这是基于其独特的寡聚动力学来决定的,该动力学决定了其特定于区室的职业。将该领域的历史与这种极其复杂的酶的多变量性质联系起来,我们进一步讨论了与DNA损伤反应,S期检查点以及最终肿瘤抑制有关的新数据的含义。我们在此希望为对这些领域感兴趣的人提供想法,并举例说明对研究RNR在生物学中的广泛作用有用的概念框架和工具。
更新日期:2019-11-01
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