LlSR28 Is Involved in Pollen Germination by Affecting Filamentous Actin Dynamics
LlSR28 Is Involved in Pollen Germination by Affecting Filamentous Actin Dynamics
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LlSR28 通过影响丝状肌动蛋白动力学参与花粉萌发
DOI：
10.1093/mp/sst097
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发表时间：
2013-07-01
期刊：
影响因子：
27.5
通讯作者：
Ren, Hai-Yun
中科院分区：
文献类型：
--
作者：
Cao, Li-Juan;Zhao, Meng-Meng;Ren, Hai-Yun
LlSR28，一种来自长花百合的丝氨酸/精氨酸丰富（SR）蛋白，我们删除了原来的句子，将其更改为改变F-肌动蛋白动力学，可能是通过其选择性剪接活性直接或间接影响AtVLN1的选择性剪接和不同肌动蛋白结合蛋白（ABP）的表达，从而影响花粉萌发。选择性剪接在花粉萌发中发挥重要作用 基因调控并有助于蛋白质复杂性。先前的研究表明，绒毛蛋白/凝溶胶蛋白/法安明超家族的成员中存在选择性剪接。在本研究中，从百合 (Lilium longiflorum) 表达文库中分离出具有 28kDa 蛋白 (LlSR28) 的富含丝氨酸/精氨酸 (SR) 蛋白 cDNA。蛋白结构域分析表明，LlSR28与拟南芥SR45（AtSR45）具有相似的结构，并且LlSR28可以补充AtSR45功能丧失的表型。因此，在以下实验中使用LlSR28和AtSR45突变体(atsr45-1)的过表达。 LlSR28在拟南芥中的过度表达完全抑制花粉萌发。相比之下，atsr45-1的花粉萌发早于野生型。此外，与野生型相比，atsr45-1花粉在花粉萌发过程中相应水合阶段含有较少的F-肌动蛋白。选择性剪接分析表明，在atst45-1中，编码全长蛋白的拟南芥villin1 (AtVLN1)转录本增加，而编码截短蛋白的转录本减少。此外，拟南芥花粉中丰富的其他肌动蛋白结合蛋白（ABP）的mRNA表达水平在atsr45-1中也发生了变化。总之，我们假设LlSR28可能通过其选择性剪接活性改变F-肌动蛋白动力学，直接或间接影响AtVLN1的选择性剪接和不同ABP的表达，从而影响花粉萌发。
LlSR28, a serine/argine-rich (SR) protein from Lilium longiflorum, We have deleted original sentence and changed it to alters F-actin dynamics probably through its alternative splicing activities to affect directly or indirectly the alternative splicing of AtVLN1 and the expression of different actin-binding proteins (ABPs), which then affects the pollen germination.Alternative splicing plays important roles in gene regulation and contributes to protein complexity. Previous studies suggest that alternative splicing exists in members of the villin/gelsolin/fragmin superfamily. In this study, a serine/argine-rich (SR) protein cDNA with 28kDa protein (LlSR28) was isolated from a lily (Lilium longiflorum) expression library. Protein domain analysis showed that LlSR28 had similar structures to Arabidopsis SR45 (AtSR45), and LlSR28 could complement the phenotype of loss of AtSR45 function. Therefore, overexpression of LlSR28 and AtSR45 mutant (atsr45-1) were used in the following experiments. Overexpression of LlSR28 in Arabidopsis completely inhibited pollen germination. In contrast, the pollen germination of atsr45-1 was earlier than that of wild-type. In addition, pollen of atsr45-1 contained less F-actin at the corresponding hydration stage during pollen germination compared to that of wild-type. Alternative splicing analysis showed that Arabidopsis villin1 (AtVLN1) transcript encoding the full-length protein was increased, and that encoding the truncated protein was decreased in atst45-1. Moreover, the mRNA expression level of other actin-binding proteins (ABPs) abundant in Arabidopsis pollen was also changed in atsr45-1. In conclusion, we hypothesize that LlSR28 alters F-actin dynamics probably through its alternative splicing activities to affect directly or indirectly the alternative splicing of AtVLN1 and the expression of different ABPs, which then affects the pollen germination.