Published online 5 October 2004
Nucleic Acids Research, Vol. 32 No. 17 © Oxford University Press 2004; all rights reserved
A novel GTPase activated by the small subunit of ribosome
1 Department of Biochemistry and Biotechnology, Faculty of Agriculture and Life Science and 2 Department of Biology, Faculty of Science, Hirosaki University, Hirosaki 036-8561, Japan, 3 The United Graduate School of Agricultural Sciences, Iwate University, Morioka 020-8550, Japan and 4 Department of Biophysics, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan
* To whom correspondence should be addressed. Tel: +81 172 39 3592; Fax: +81 172 39 3593; Email: himeno{at}cc.hirosaki-u.ac.jp
Present addresses: Kyoko Hanawa-Suetsugu, RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan
Liliya Kalachnyuk, Biotechnology Research, Institute of Animal Production, S.Z. Gzhytskyi Lviv Academy of Veterinary Medicine, 50 Pekarska Street, Lviv 79010, Ukraine
Received August 26, 2004; Revised and Accepted September 14, 2004
The GTPase activity of Escherichia coli YjeQ, here named RsgA (ribosome small subunit-dependent GTPase A), has been shown to be significantly enhanced by ribosome or its small subunit. The enhancement of GTPase activity was inhibited by several aminoglycosides bound at the A site of the small subunit, but not by a P site-specific antibiotic. RsgA stably bound the small subunit in the presence of GDPNP, but not in the presence of GTP or GDP, to dissociate ribosome into subunits. Disruption of the gene for RsgA from the genome affected the growth of the cells, which predominantly contained the dissociated subunits having only a weak activation activity of RsgA. We also found that 17S RNA, a putative precursor of 16S rRNA, was contained in the small subunit of the ribosome from the RsgA-deletion strain. RsgA is a novel GTPase that might provide a new insight into the function of ribosome.
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