E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides.

E. coli HflX interacts with 50S ribosomal subunits in presence of nucleotides.
复制标题

在存在核苷酸的情况下,大肠杆菌HFLX与50S核糖体亚基相互作用。

DOI:
10.1016/j.bbrc.2008.12.072
复制
发表时间:
2009-02-06
影响因子:
3.1
通讯作者:
Prakash, Balaji
Prakash, Balaji
中科院分区:
生物学4区
文献类型:
--
作者:
Jain, Nikhil;Dhimole, Neha;Khan, Abu Rafay;De, Debojyoti;Tomar, Sushil Kumar;Sajish, Mathew;Dutta, Dipak;Parrack, Pradeep;Prakash, Balaji

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HflX是一种功能未知的GTP结合蛋白。根据hflA操纵子中hflX基因的存在,hflX被认为参与了大肠杆菌噬菌体感染过程中的裂解-溶源决定。我们发现大肠杆菌HflX结合了16S和23S rRNA-30S和50S核糖体亚基的RNA成分。在这里,使用纯化的核糖体亚基,我们证明了HflX与50s特异地相互作用。这一发现与参与核糖体生物发生的GTP酶的HflX同源性是一致的。然而,HflX-50s的相互作用并不局限于蛋白质的特定核苷酸结合状态,并且任何核苷酸GTP/GDP/ATP/ADP的存在就足够了。在这一点上,HflX不同于其他GTP酶。而大肠杆菌HflX结合并水解三磷酸腺苷和GTP,只有GTP水解酶活性受到50S结合的刺激。这项工作揭示了HflX在核糖体结合中的有趣属性。
HflX is a GTP binding protein of unknown function. Based on the presence of the hflX gene in hflA operon, HflX was believed to be involved in the lytic-lysogenic decision during phage infection in Escherichia coli. We find that E. coli HflX binds 16S and 23S rRNA – the RNA components of 30S and 50S ribosomal subunits. Here, using purified ribosomal subunits, we show that HflX specifically interacts with the 50S. This finding is in line with the homology of HflX to GTPases involved in ribosome biogenesis. However, HflX-50S interaction is not limited to a specific nucleotide-bound state of the protein, and the presence of any of the nucleotides GTP/GDP/ATP/ADP is sufficient. In this respect, HflX is different from other GTPases. While E. coli HflX binds and hydrolyses both ATP and GTP, only the GTP hydrolysis activity is stimulated by 50S binding. This work uncovers interesting attributes of HflX in ribosome binding.
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