Mobilization of storage proteins in soybean seed (Glycine max L.) during germination and seedling growth
Mobilization of storage proteins in soybean seed (Glycine max L.) during germination and seedling growth
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DOI：
10.1016/j.bbapap.2011.05.004
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发表时间：
2011-09-01
影响因子：
3.2
通讯作者：
Kwon, Oh-Shin
中科院分区：
文献类型：
--
作者：
Kim, Hyun Tae;Choi, Ung-Kyu;Kwon, Oh-Shin
在种子萌发和幼苗早期生长过程中，贮藏蛋白被蛋白酶降解。目前，有限的信息是在大豆发芽过程中的贮藏蛋白质的降解。在这项研究中，结合双向凝胶电泳和质谱法的方法来确定大豆种子（Glycine max L; Eunhakong）的蛋白质组图谱。比较分析表明，在种子萌发和幼苗生长过程中，蛋白质表达的时间分布发生了显著变化。超过80%的蛋白质鉴定的大豆球蛋白和β-伴大豆球蛋白，两个主要的存储蛋白的亚基。这些蛋白质的大多数亚基在120 h时几乎完全以不同的速率降解，并且降解产物进一步积累或降解。有趣的是，大豆球蛋白的酸性亚基迅速降解，但基本链没有明显的变化。在5种酸性亚基中，G2亚基的降解至少在96 h内不受明显影响，但在96 h后迅速下降，而G4亚基降解后未检测到新的中间产物。另一方面，β-伴大豆球蛋白在贮存蛋白动员过程中的降解似乎与大豆球蛋白的降解相似，但速率更快。β-伴大豆球蛋白的α和α '亚基在96 h时基本消失，而β亚基以最慢的速率降解。这些结果表明，种子萌发和幼苗生长的存储蛋白的亚基的动员差异调节。目前的蛋白质组学分析将有助于解决大豆种子萌发过程中发生的复杂的生化事件的未来研究。(C)2011 Elsevier B. V.保留所有权利。
During germination and early growth of the seedling, storage proteins are degraded by proteases. Currently, limited information is available on the degradation of storage proteins in the soybean during germination. In this study, a combined two-dimensional gel electrophoresis and mass spectrometry approach was utilized to determine the proteome profile of soybean seeds (Glycine max L; Eunhakong). Comparative analysis showed that the temporal profiles of protein expression are dramatically changed during the seed germination and seedling growth. More than 80% of the proteins identified were subunits of glycinin and beta-conglycinin, two major storage proteins. Most subunits of these proteins were degraded almost completely at a different rate by 120 h, and the degradation products were accumulated or degraded further. Interestingly, the acidic subunits of glycinin were rapidly degraded, but no obvious change in the basic chains. Of the five acidic subunits, the degradation of G2 subunit was not apparently affected by at least 96 h but the levels decreased rapidly after that, while no newly appearing intermediate was detected upon the degradation of G4 subunit. On the other hand, the degradation of beta-conglycinin during storage protein mobilization appeared to be similar to that of glycinin but at a faster rate. Both alpha and alpha' subunits of beta-conglycinin largely disappeared by 96 h, while the beta subunits degraded at the slowest rate. These results suggest that mobilization of subunits of the storage proteins is differentially regulated for seed germination and seedling growth. The present proteomic analysis will facilitate future studies addressing the complex biochemical events taking place during soybean seed germination. (C) 2011 Elsevier B.V. All rights reserved.