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¹ Department of Physics, Osaka Medical College, Takatsuki, Osaka 569-8686, Japan
² Laboratory of Plasma Membrane and Nuclear Signaling, Graduate School of Biostudies, Kyoto University, Kitashirakawa-Oiwake, Sakyo-ku, Kyoto 606-8502, Japan
³ Institute of Advanced Biosciences, Keio University, Tsuruoka, Yamagata 997-0035, Japan
⁴ Research and Education Center of Informatics, Nara Institute of Science and Technology, Ikoma, Nara 630-0101, Japan

During the stationary phase of Escherichia coli growth, ribosomal structure changes drastically. Proteins RMF, YhbH, YfiA and SRA are expressed and bind to ribosome particles. In a process named ‘ribosomal hibernation,’ RMF binding induces the dimerization and subsequent inactivation of 70S ribosomes. Here, we examined the functions of YhbH and YfiA in the formation of 70S dimers using deletion mutants of YhbH and YfiA. The yfiA deletion mutant expressed YhbH and RMF in the stationary phase and formed a greater number of 100S particles than the wild-type, showing that YhbH promotes and stabilizes 100S formation. In contrast, the yhbH deletion mutant expressed YfiA and RMF and produced no 70S dimers, suggesting that YfiA prevents 70S dimer formation. Thus, YhbH and YfiA have opposite functions in 70S dimer formation. YhbH and YfiA share 40% sequence homology, suggesting that their binding sites overlap and they compete for a region proximal to the P- and A-sites on 30S subunits. In the yhbH and yfiA double deletion mutant, which expresses only RMF, 70S dimers were observed as 90S particles. Since 100S particles were seen in the yfiA deletion mutant containing RMF and YhbH, YhbH probably converts immature 90S ribosomes into mature 100S particles.

^aPresent address: Department of Physics, Osaka Medical College, 2-7, Daigaku-Machi, Takatsuki, Osaka 569-8686, Japan. E-mail: phy003{at}art.osaka-med.ac.jp

^* Correspondence: E-mail: phy003{at}art.osaka-med.ac.jp

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