Bacillus subtilis aconitase is an RNA-binding protein
Bacillus subtilis aconitase is an RNA-binding protein
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DOI：
10.1073/pnas.96.18.10412
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发表时间：
1999-08-31
影响因子：
11.1
通讯作者：
Sonenshein, AL
中科院分区：
文献类型：
--
作者：
Alén, C;Sonenshein, AL
芽孢杆菌的顺乌头酸酶蛋白能够特异性地结合类似于真核生物mRNA中发现的铁反应元件（IRE）的序列。结合的序列包括编码主要细胞色素氧化酶和铁摄取系统的B：subtilis操纵子中的兔铁蛋白IRE和IRE样序列。IRE结合活性受体内和体外铁的可用性的影响。在真核细胞中，乌头酸酶样蛋白调节铁代谢mRNA的翻译和稳定性以响应铁的可用性，B的突变株。枯草芽孢杆菌产生的酶失活的乌头酸酶，仍然能够结合RNA孢子化40倍更有效地比乌头酸酶无效突变体，这表明乌头酸酶的非酶活性是重要的孢子形成。结果支持这样的想法，细菌乌头酸酶，像它们的真核同源物，是双功能蛋白质，显示乌头酸酶活性在铁和RNA结合活性的存在下，当细胞被铁剥夺。
The aconitase protein of Bacillus sabtilis was able to bind specifically to sequences resembling the iron response elements (IREs) found in eukaryotic mRNAs, The sequences bound include the rabbit ferritin IRE and IRE-like sequences in the B: subtilis operons that encode the major cytochrome oxidase and an iron uptake system. IRE binding activity was affected by the availability of iron both in vivo and in vitro . In eukaryotic cells, aconitase-like proteins regulate translation and stability of iron metabolism mRNAs in response to iron availability, A mutant strain of B. subtilis that produces an enzymatically inactive aconitase that was still able to bind RNA sporulated 40 x more efficiently than did an aconitase null mutant, suggesting that a nonenzymatic activity of aconitase is important for sporulation. The results support the idea that bacterial aconitases, like their eukaryotic homologs, are bifunctional proteins, showing aconitase activity in the presence of iron and RNA binding activity when cells are iron-deprived.