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J. Biol. Chem., Vol. 282, Issue 35, 25270-25277, August 31, 2007

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Isolation and Characterization of a Dominant Negative Mutant of Bacillus subtilis GTP-binding Protein, YlqF, Essential for Biogenesis and Maintenance of the 50 S Ribosomal Subunit^*

From the Department of Bioinformatics and Genomics, Graduate School of Information Science, Nara Institute of Science and Technology, 8916-5, Takayama, Ikoma, Nara 630-0101, Japan

The circularly permuted GTPase YlqF is essential for cell viability and is broadly conserved from Gram-positive bacteria to eukaryotes. We previously reported that YlqF participates in the late step of 50 S ribosomal subunit assembly in Bacillus subtilis. Here, we demonstrate that an N-terminal deletion mutant of YlqF (YlqFN10) inhibits cell growth even in the presence of wild-type YlqF. In contrast to the wild-type protein, the GTPase activity of this mutant was not stimulated by the 50 S subunit and did not dissociate from the premature 50 S subunit. Thus, YlqFN10 acts as a competitive inhibitor of wild-type YlqF. Premature 50 S subunit lacking ribosomal protein L27 and with a reduced amount of L16 accumulated in YlqFN10-overexpressing cells and in YlqF-depleted cells, suggesting that YlqFN10 binds to the premature 50 S subunit. Moreover, premature 50 S subunit from both YlqFN10-overexpressing and YlqF-depleted cells more strongly enhanced the GTPase activity of YlqF than the mature 50 S subunit of the 70 S ribosome. Collectively, our results indicate that YlqF is targeted to the premature 50 S subunit lacking ribosomal proteins L16 and L27 to assemble functional 50 S subunit through a GTPase activity-dependent conformational change of 23 S rRNA.

Received for publication, May 11, 2007 , and in revised form, July 5, 2007.

^* This work was supported by a KAKENHI grant-in-aid for scientific research on Priority Area "Systems Genomics" from the Ministry of Education, Culture, Sports, Science, and Technology of Japan and Grant-in-Aid for Scientific Research (A) 17201040 from the Japan Society for Promotion of Sciences. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom all correspondence should be addressed. Tel.: 81-743-72-5430; Fax: 81-743-72-5439; E-mail: nogasawa{at}bs.naist.jp.

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