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Journal of Bacteriology, May 2002, p. 2595-2602, Vol. 184, No. 10
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.10.2595-2602.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Proteolytic Activity of YibP Protein in Escherichia coli

Toshiharu Ichimura,¹ Mitsuyoshi Yamazoe,^1, Maki Maeda,² Chieko Wada,² and Sota Hiraga^1*

Division of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University, Kuhonji 4-24-1, Kumamoto 862-0976,¹ Department of Cell Biology, Institute for Virus Research, Kyoto University, Shogoin-kawaracho, Sakyoku, Kyoto 606-8507, Japan²

Received 26 November 2001/ Accepted 11 February 2002

Escherichia coli YibP protein (47.4 kDa) has a membrane-spanning signal at the N-terminal region, two long coiled-coil regions in the middle part, and a C-terminal globular domain, which involves amino acid sequences homologous to the peptidase M23/M37 family. A yibP disrupted mutant grows in rich medium at 37°C but not at 42°C. In the yibP null mutant, cell division and FtsZ ring formation are inhibited at 42°C without SOS induction, resulting in filamentous cells with multiple nucleoids and finally in cell lysis. Five percent betaine suppresses the temperature sensitivity of the yibP disrupted mutation. The mutant has the same sensitivity to drugs, such as nalidixic acid, ethidium bromide, ethylmethane sulfonate, and sodium dodecyl sulfate, as the parental strain. YibP protein is recovered in the inner membrane and cytoplasmic fractions, but not in the outer membrane fraction. Results suggest that the coiled-coil regions and the C-terminal globular domain of YibP are localized in the cytoplasmic space, not in the periplasmic space. Purified YibP has a protease activity that split the substrate ß-casein.

Present address: Department of Radiation Genetics, Kyoto University, Konoe, Yoshida, Sakyoku, Kyoto 606-8501, Japan.

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