A two-staged model of Na+ exclusion in rice explained by 3D modeling of HKT transporters and alternative splicing.

A two-staged model of Na+ exclusion in rice explained by 3D modeling of HKT transporters and alternative splicing.
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DOI:
10.1371/journal.pone.0039865
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
Hrmova M
Hrmova M
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Cotsaftis O;Plett D;Shirley N;Tester M;Hrmova M

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Na+和Na+/K+转运体HKT家族与植物耐盐性有关。在这些转运蛋白中,谷类HKT1;4及HKT1;5个基因负责从光合组织中排除Na+,这是植物耐盐的关键机制。有研究认为,Na+可以从根或叶鞘的木质部蒸腾流中获取,从而保护叶片免受Na+的过量积累。然而,这种情况的直接证据很少。基于细菌TrkH K+转运体最新晶体结构的水稻(Oryza sativa) hkt转运体的比较建模和评估允许协调转录组学和生理数据。OsHKT1;5、选择性过滤器内转录物丰度和蛋白质结构特征都能控制水稻品种茎部Na+积累。OsHKT1;4、需要考虑转录物的选择性剪接和鞘的解剖复杂性。因此,Na+在特定叶片中的积累似乎受到正确剪接的OsHKT1丰度的调节;在相应鞘中的转录本。总的来说,叶片Na+积累的等位基因变异可以通过基因转录、选择性剪接和蛋白质结构的复杂相互作用来解释。
The HKT family of Na+ and Na+/K+ transporters is implicated in plant salinity tolerance. Amongst these transporters, the cereal HKT1;4 and HKT1;5 are responsible for Na+ exclusion from photosynthetic tissues, a key mechanism for plant salinity tolerance. It has been suggested that Na+ is retrieved from the xylem transpiration stream either in the root or the leaf sheath, protecting the leaf blades from excessive Na+ accumulation. However, direct evidence for this scenario is scarce. Comparative modeling and evaluation of rice (Oryza sativa) HKT-transporters based on the recent crystal structure of the bacterial TrkH K+ transporter allowed to reconcile transcriptomic and physiological data. For OsHKT1;5, both transcript abundance and protein structural features within the selectivity filter could control shoot Na+ accumulation in a range of rice varieties. For OsHKT1;4, alternative splicing of transcript and the anatomical complexity of the sheath needed to be taken into account. Thus, Na+ accumulation in a specific leaf blade seems to be regulated by abundance of a correctly spliced OsHKT1;4 transcript in a corresponding sheath. Overall, allelic variation of leaf blade Na+ accumulation can be explained by a complex interplay of gene transcription, alternative splicing and protein structure.
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