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Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern
Nature Chemical Biology ( IF 14.8 ) Pub Date : 2018-06-11 , DOI: 10.1038/s41589-018-0077-5
Benoit Castrec , Cyril Dian , Sarah Ciccone , Coralie L. Ebert , Willy V. Bienvenut , Jean-Pierre Le Caer , Jean-Marc Steyaert , Carmela Giglione , Thierry Meinnel

An organism’s entire protein modification repertoire has yet to be comprehensively mapped. N-myristoylation (MYR) is a crucial eukaryotic N-terminal protein modification. Here we mapped complete Homo sapiens and Arabidopsis thaliana myristoylomes. The crystal structures of human modifier NMT1 complexed with reactive and nonreactive target-mimicking peptide ligands revealed unexpected binding clefts and a modifier recognition pattern. This information allowed integrated mapping of myristoylomes using peptide macroarrays, dedicated prediction algorithms, and in vivo mass spectrometry. Global MYR profiling at the genomic scale identified over a thousand novel, heterogeneous targets in both organisms. Surprisingly, MYR involved a non-negligible set of overlapping targets with N-acetylation, and the sequence signature marks for a third proximal acylation—S-palmitoylation—were genomically imprinted, allowing recognition of sequences exhibiting both acylations. Together, the data extend the N-end rule concept for Gly-starting proteins to subcellular compartmentalization and reveal the main neighbors influencing protein modification profiles and consequent cell fate.



中文翻译:

人类和植物肉豆蔻组的结构和基因组解码揭示了确定的识别模式

一个生物体的整个蛋白质修饰库尚未被全面绘制。N-豆蔻酰化(MYR)是至关重要的真核N末端蛋白修饰。在这里,我们绘制了完整的智人和拟南芥肉豆蔻。人类修饰剂NMT1的晶体结构与反应性和非反应性的模拟靶标肽配体复合显示出意外的结合裂隙和修饰剂识别模式。该信息允许使用肽大分子阵列,专用预测算法和体内质谱对肉豆蔻菌丝组进行整合定位。基因组规模的全球MYR谱图鉴定了两种生物中的一千多种新型异质靶标。出人意料的是,MYR涉及一组不可忽略的带有N-乙酰化的重叠靶标,并且基因组学上印有第三个近端酰化作用(S-棕榈酰化)的序列特征标记,从而可以识别显示两种酰化作用的序列。一起,

更新日期:2018-06-12
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