¹H, ¹³C, ¹⁵N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the HvGR-RBP1 protein involved in the regulation of barley (Hordeum vulgare L.) senescence.

¹H, ¹³C, ¹⁵N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the HvGR-RBP1 protein involved in the regulation of barley (Hordeum vulgare L.) senescence.
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DOI:
10.1007/s12104-013-9472-8
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发表时间:
2014-04
影响因子:
0.9
通讯作者:
Copié V
Copié V
中科院分区:
生物学4区
文献类型:
--
作者:
Mason KE;Tripet BP;Parrott D;Fischer AM;Copié V

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叶片衰老是植物生命发育过程中的一个重要过程。衰老效率影响重要的农业性状,如籽粒蛋白质含量和植物生长,这往往是由氮素利用的限制。人们对调节这一高度协调的过程的分子机制知之甚少。为了加强我们对叶片衰老及其调控的理解,我们对大麦(Hordeum vulgare L.)中参与衰老控制的以前未知的蛋白质进行了结构和功能表征。先前的微阵列分析突出了几个大麦基因,其转录物在衰老期间差异表达,包括一个特定的基因,其在开花后14天和21天(开花期)与晚衰老近等基因大麦系相比,在早期旗叶中上调超过40倍。通过检查其氨基酸序列,预测该基因编码富含甘氨酸的RNA结合蛋白,在本文中称为HvGR-RBP 1。HvGR-RBP 1已在大肠杆菌中表达。初步的NMR数据分析表明,其富含甘氨酸的C-末端区域[残基:93-162]在结构上是无序的,而其N-末端区域[残基:1-92]形成良好折叠的结构域。在此,我们报告了完整的1H,13 C和15 N共振分配的骨干和侧链原子,和二级结构拓扑结构的N-末端RNA识别基序(RRM)域的HvGR-RBP 1,作为第一步,解开其结构和功能的作用,在大麦叶片衰老的调节。
Leaf senescence is an important process in the developmental life of all plant species. Senescence efficiency influences important agricultural traits such as grain protein content and plant growth, which are often limited by nitrogen use. Little is known about the molecular mechanisms regulating this highly orchestrated process. To enhance our understanding of leaf senescence and its regulation, we have undertaken the structural and functional characterization of previously unknown proteins that are involved in the control of senescence in barley (Hordeum vulgare L.). Previous microarray analysis highlighted several barley genes whose transcripts are differentially expressed during senescence, including a specific gene which is greater than 40 fold up-regulated in the flag leaves of early- as compared to late-senescing near-isogenic barley lines at 14 and 21 days past flowering (anthesis). From inspection of its amino acid sequence, this gene is predicted to encode a glycine-rich RNA-binding protein herein referred to as HvGR-RBP1. HvGR-RBP1 has been expressed as a recombinant protein in E. coli, and preliminary NMR data analysis has revealed that its glycine-rich C-terminal region [residues: 93–162] is structurally disordered whereas its N-terminal region [residues: 1–92] forms a well-folded domain. Herein, we report the complete 1H, 13C, and 15N resonance assignments of backbone and sidechain atoms, and the secondary structural topology of the N-terminal RNA Recognition Motif (RRM) domain of HvGR-RBP1, as a first step to unraveling its structural and functional role in the regulation of barley leaf senescence.
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