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

被引：40

作者：

Jain, Nikhil ^{[1
]}

Dhimole, Neha ^{[1
]}

Khan, Abu Rafay ^{[1
]}

De, Debojyoti ^{[1
]}

Tomar, Sushil Kumar ^{[1
]}

Sajish, Mathew ^{[1
]}

Dutta, Dipak ^{[2
]}

Parrack, Pradeep ^{[2
]}

Prakash, Balaji ^{[1
]}

机构：

[1] Indian Inst Technol, Dept Biol Sci & Bioengn, Kanpur 208016, Uttar Pradesh, India

[2] Bose Inst, Dept Biochem, Kolkata 700054, India

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2009年 / 379卷 / 02期

基金：

英国惠康基金;

关键词：

Hflx; GTPase; ATPase; rRNA binding protein; Ribosome binding GTPase; Ribosome assembly; ESCHERICHIA-COLI; BACILLUS-SUBTILIS; GTPASE ACTIVITY; BINDING; RNA; ERA;

D O I：

10.1016/j.bbrc.2008.12.072

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2008 Elsevier Inc. All rights reserved.

引用

页码：201 / 205

页数：5

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