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Originally published In Press as doi:10.1074/jbc.M208564200 on December 17, 2002

J. Biol. Chem., Vol. 278, Issue 8, 5902-5911, February 21, 2003
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Genetic and Biochemical Characterization of EshA, a Protein That Forms Large Multimers and Affects Developmental Processes in Streptomyces griseus*

Natsumi Saito, Keiko MatsubaraDagger , Masakatsu Watanabe§, Fumio Kato, and Kozo Ochi||

From the National Food Research Institute, Tsukuba, Ibaraki 305-8642, Japan

The 52-kDa protein, EshA, whose expression is controlled developmentally, is produced during the late growth phase of Streptomyces spp. We found that disruption of the eshA gene, which encodes the EshA protein, abolishes the aerial mycelium formation and streptomycin production in Streptomyces griseus when grown on an agar plate. The eshA disruptant KO-390 demonstrated a reduced amount of expression of the transcriptional activator strR, thus accounting for the failure to produce streptomycin. KO-390 was found to accumulate deoxynucleoside triphosphates at high levels, including dGTP, at late growth phase. The accumulation of dGTP was a cause for the impaired ability of KO-390 to produce aerial mycelium, because the ability to form aerial mycelium was completely repaired by addition of decoyinine, an inhibitor of GMP synthetase. The accumulation of dNTP in KO-390 coincided with a reduced rate of DNA synthesis. The developmental time frame of these phenomena in KO-390 matched a burst of EshA expression in the wild-type strain. In contrast to S. griseus, the eshA disruption did not affect the ability for Streptomyces coelicolor to form aerial mycelium and did not result in the aberrant accumulation of dNTP accompanied by arrest of DNA synthesis, implying qualitative differences in addition to quantitative differences between the two EshA proteins. We propose that the S. griseus EshA protein somehow positively affects (or regulates) the replication of DNA in wild-type cells at late growth phase but leads to aberrant phenotypes in mutant cells due to the disturbed DNA replication. The EshA protein was found to exist as a multimer (~20-mers) creating a cubic-like structure with a diameter of 27 nm and located predominantly in cytoplasm.


* This work was supported in part by a grant from the Organized Research Combination System of the Science and Technology Agency of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Translational Research Department, Mitsubishi Kagaku Institute of Life Sciences, Yokohama Research Center, 1000, Kamoshida-cho, Aoba-ku, Yokohama, Kanagawa 227-8502, Japan.

§ Present address: Dept. of Biological Science, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuda-Cho, Midori-ku, Yokohama 226-8501, Japan.

Present address: Dept. of Microbiology, School of Pharmaceutical Sciences, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8501, Japan.

|| To whom correspondence should be addressed: National Food Research Institute, 2-1-12 Kannondai, Tsukuba, Ibaraki 305-8642, Japan. Tel.: 81-29-838-8125; Fax: 81-29-838-7996; E-mail: kochi@affrc.go.jp.


Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.


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