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
中科院分区:
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
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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影响因子:
3.2
作者:
Daigle, DM;Brown, ED
通讯作者:
Brown, ED
DOI:
10.1083/jcb.146.4.723
发表时间:
1999-08-23
期刊:
The Journal of cell biology
影响因子:
--
作者:
Bacher G;Pool M;Dobberstein B
通讯作者:
Dobberstein B
影响因子:
5.3
作者:
Pertschy, Brigitte;Saveanu, Cosmin;Bergler, Helmut
通讯作者:
Bergler, Helmut
影响因子:
16
作者:
Sharma, MR;Barat, C;Agrawal, RK
通讯作者:
Agrawal, RK
影响因子:
2.8
作者:
Polkinghorne, Adam;Ziegler, Urs;Vaughan, Lloyd
通讯作者:
Vaughan, Lloyd