Uncoiling CNLs: Structure/Function Approaches to Understanding CC Domain Function in Plant NLRs.

Uncoiling CNLs: Structure/Function Approaches to Understanding CC Domain Function in Plant NLRs.
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DOI:
10.1093/pcp/pcy185
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发表时间:
2018-12-01
影响因子:
4.9
通讯作者:
Banfield MJ
Banfield MJ
中科院分区:
生物学2区
文献类型:
--
作者:
Bentham AR;Zdrzalek R;De la Concepcion JC;Banfield MJ

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植物核苷酸结合富亮氨酸重复序列受体(NLR)是一类细胞内病原体受体,其N端结构域在病原体衍生的效应蛋白感知后的信号转导中是不可或缺的。两种主要的植物NLR类别通过在其N-末端存在Toll/白细胞介素-1受体(TIR)或卷曲螺旋(CC)结构域(TNL和CNL)来定义。我们对CC结构域在植物CNLs中的功能的了解落后于TIR结构域在植物TNL中的功能。CNLs是单子叶植物中最丰富的一类NLR,需要进一步研究以了解这些结构域如何有助于谷类作物抗病性的分子机制。以前的CC结构域的研究已经揭示了功能的多样性,分类困难,这反过来又使实验设计的功能测定具有挑战性。在这篇综述中,我们总结了目前对植物CNLs中CC结构域功能的理解,突出了作用方式和结构的差异。为了帮助探索CC结构域功能的实验设计,我们提出了一个“最佳实践”的指导,通过使用序列和二级结构的比较,设计结构,并讨论了相关的检测CC结构域功能的调查。最后,我们讨论了是否使用同源建模是有用的,以描述假定的CC结构域的功能,通过与先前表征的螺旋衔接蛋白的功能的平行CNLs。
Plant nucleotide-binding leucine-rich repeat receptors (NLRs) are intracellular pathogen receptors whose N-terminal domains are integral to signal transduction after perception of a pathogen-derived effector protein. The two major plant NLR classes are defined by the presence of either a Toll/interleukin-1 receptor (TIR) or a coiled-coil (CC) domain at their N-terminus (TNLs and CNLs). Our knowledge of how CC domains function in plant CNLs lags behind that of how TIR domains function in plant TNLs. CNLs are the most abundant class of NLRs in monocotyledonous plants, and further research is required to understand the molecular mechanisms of how these domains contribute to disease resistance in cereal crops. Previous studies of CC domains have revealed functional diversity, making categorization difficult, which in turn makes experimental design for assaying function challenging. In this review, we summarize the current understanding of CC domain function in plant CNLs, highlighting the differences in modes of action and structure. To aid experimental design in exploring CC domain function, we present a ‘best-practice’ guide to designing constructs through use of sequence and secondary structure comparisons and discuss the relevant assays for investigating CC domain function. Finally, we discuss whether using homology modeling is useful to describe putative CC domain function in CNLs through parallels with the functions of previously characterized helical adaptor proteins.
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