Profiling of the Candidate Interacting Proteins of SELF-PRUNING 6A (SP6A) in Solanum tuberosum.
Profiling of the Candidate Interacting Proteins of SELF-PRUNING 6A (SP6A) in Solanum tuberosum.
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DOI：
10.3390/ijms23169126
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发表时间：
2022-08-15
影响因子：
5.6
通讯作者：
中科院分区：
文献类型：
--
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自修剪6A（SELF-PRUNING 6A，SP 6A）是马铃薯中一个与FLOW LOCUS T（FT）同源的基因，被鉴定为块茎原。StSP 6A是一种移动的信号，在马铃薯叶片中合成，并通过韧皮部传递到匍匐茎，在马铃薯生长发育过程中发挥着多重作用。然而，马铃薯中的全球StSP 6A蛋白相互作用网络仍然知之甚少。本研究首次以BK-StSP 6A为诱饵，通过筛选马铃薯酵母双杂交（Y2 H）文库，研究了StSP 6A相互作用网络，筛选出200个独立的阳性克隆，鉴定出77个相互作用蛋白。然后，通过Y2 H和BiFC试验进一步证实StSP 6A与其相互作用子之间的相互作用，并选择三个相互作用子进行进一步的表达分析。最后，研究了开花促进因子1.1（StFPF1.1）、短日不开花（StNFL 1和StNFL 2）的表达模式。这三个基因在花或花蕾中均高表达。StFPF1.1在匍匐茎膨大期表现出与StSP 6A相似的表达模式。StPHYF沉默的植物表现出StFPF1.1和StSP 6A的表达上调，而StNFL 1和StNFL 2的表达在匍匐茎中下调。这些相互作用蛋白的鉴定为进一步研究StSP 6A的功能奠定了坚实的基础。
SELF-PRUNING 6A (SP6A), a homolog of FLOWERING LOCUS T (FT), has been identified as tuberigen in potato. StSP6A is a mobile signal synthesized in leaves and transmitted to the stolon through phloem, and plays multiple roles in the growth and development of potato. However, the global StSP6A protein interaction network in potato remains poorly understood. In this study, BK-StSP6A was firstly used as the bait to investigate the StSP6A interaction network by screening the yeast two-hybrid (Y2H) library of potato, resulting in the selection of 200 independent positive clones and identification of 77 interacting proteins. Then, the interaction between StSP6A and its interactors was further confirmed by the Y2H and BiFC assays, and three interactors were selected for further expression analysis. Finally, the expression pattern of Flowering Promoting Factor 1.1 (StFPF1.1), No Flowering in Short Days 1 and 2 (StNFL1 and StNFL2) was studied. The three genes were highly expressed in flowers or flower buds. StFPF1.1 exhibited an expression pattern similar to that of StSP6A at the stolon swelling stages. StPHYF-silenced plants showed up-regulated expression of StFPF1.1 and StSP6A, while expression of StNFL1 and StNFL2 was down-regulated in the stolon. The identification of these interacting proteins lays a solid foundation for further functional studies of StSP6A.
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