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Journal of Bacteriology, April 2006, p. 2715-2720, Vol. 188, No. 7
0021-9193/06/$08.00+0     doi:10.1128/JB.188.7.2715-2720.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Liberation of Zinc-Containing L31 (RpmE) from Ribosomes by Its Paralogous Gene Product, YtiA, in Bacillus subtilis

Genki Akanuma, Hideaki Nanamiya, Yousuke Natori, Naofumi Nomura, and Fujio Kawamura*

Laboratory of Molecular Genetics and Frontier Project "Life's Adaptation Strategies to Environmental Changes," Department of Life Science, College of Science, Rikkyo University, Toshima-ku, Tokyo 171-8501, Japan

Received 28 October 2005/ Accepted 13 January 2006

We have found that alternative localization of two types of L31 ribosomal protein, RpmE and YtiA, is controlled by the intracellular concentration of zinc in Bacillus subtilis. The detailed mechanisms for the alternation of L31 proteins under zinc-deficient conditions were previously unknown. To obtain further information about this regulatory mechanism, we have studied the stability of RpmE in vivo and the binding affinity of these proteins to ribosomes in vitro, and we have found that liberation of RpmE from ribosomes is triggered by the expression of ytiA, which is induced by the derepression of Zur under zinc-deficient conditions.

* Corresponding author. Mailing address: College of Science, Rikkyo University, Toshima-ku Nishi-ikebukuro 3-34-1, Tokyo 171-8501, Japan. Phone and fax: 81-3-3985-2401. E-mail: kawamura{at}rikkyo.ne.jp.

Journal of Bacteriology, April 2006, p. 2715-2720, Vol. 188, No. 7
0021-9193/06/$08.00+0     doi:10.1128/JB.188.7.2715-2720.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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