L-Arginine influences the structure and function of arginase mRNA in Aspergillus nidulans
L-Arginine influences the structure and function of arginase mRNA in Aspergillus nidulans
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DOI：
10.1515/bc.2007.015
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发表时间：
2007-02-01
影响因子：
3.7
通讯作者：
Weglenski, Piotr
中科院分区：
文献类型：
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作者：
Borsuk, Piotr;Przykorska, Anna;Weglenski, Piotr
精氨酸酶结构基因（agaA）的表达受到复杂的转录和转录后调控。精氨酸酶mRNA具有长5'-UTR序列。对该序列的硅分析揭示了其复杂的二级结构，存在精氨酸结合基序（精氨酸适配体）和一个具有两个潜在3'剪接位点的短内含子。在本报告中，我们提出证据表明，l -精氨酸(i)直接与精氨酸酶5'-UTR结合；（ii）与其他l -氨基酸和d -精氨酸不同，它会引起5'-UTR二级结构的剧烈变化；以及（iii）强制选择存在于5‘-UTR中的内含子的两个3’剪接位点中的一个。我们假设，真核结构基因编码精氨酸酶的表达在A. nidulans的mRNA稳定性水平上受到调节，这取决于核糖体开关介导的5'-UTR内含子的选择性剪接。
Expression of the arginase structural gene (agaA) in Aspergillus nidulans is subject to complex transcriptional and post-transcriptional regulation. Arginase mRNA has a long 5'-UTR sequence. Analysis of this sequence in silico revealed its putative complex secondary structure, the presence of arginine-binding motifs (arginine aptamers) and a short intron with two potential 3' splicing sites. In this report we present evidence that L-arginine (i) binds directly to the arginase 5'-UTR; (ii) invokes drastic changes in the secondary structure of the 5'-UTR, unlike several other L-amino acids and D-arginine; and (iii) forces the selection of one of two 3' splice sites of an intron present in the 5'-UTR. We postulate that expression of the eukaryotic structural gene coding for arginase in A. nidulans is regulated at the level of mRNA stability, depending on riboswitch-mediated alternative splicing of the 5'-UTR intron.