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  1. 020 学位論文
  2. 生命科学研究科
  3. 18 遺伝学専攻

Structural and Functional Modulations of RNApolymerase During Growth Phase Transition ofEscherichia coli

https://ir.soken.ac.jp/records/879
https://ir.soken.ac.jp/records/879
80b95296-92cf-4367-b010-335c3af57c08
名前 / ファイル ライセンス アクション
甲18_要旨.pdf 要旨・審査要旨 / Abstract, Screening Result (189.5 kB)
Item type 学位論文 / Thesis or Dissertation(1)
公開日 2010-02-22
タイトル
タイトル Structural and Functional Modulations of RNApolymerase During Growth Phase Transition ofEscherichia coli
タイトル
タイトル Structural and Functional Modulations of RNApolymerase During Growth Phase Transition ofEscherichia coli
言語 en
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_46ec
資源タイプ thesis
著者名 尾崎, 美和子

× 尾崎, 美和子

尾崎, 美和子

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フリガナ オザキ, ミワコ

× オザキ, ミワコ

オザキ, ミワコ

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著者 OZAKI, Miwako

× OZAKI, Miwako

en OZAKI, Miwako

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学位授与機関
学位授与機関名 総合研究大学院大学
学位名
学位名 博士(理学)
学位記番号
内容記述タイプ Other
内容記述 総研大甲第18号
研究科
値 生命科学研究科
専攻
値 18 遺伝学専攻
学位授与年月日
学位授与年月日 1992-03-16
学位授与年度
値 1991
要旨
内容記述タイプ Other
内容記述 During the growth phase transition of <u>Escherichia</u> <u>coli</u> from exponential<br /> growth to stationary phase, the pre-existing RNA polymerase was found to be<br /> converted into at least three different holoenzyme forms, which could be<br /> isolated by phosphocellulose column chromatography (Ozaki, M., <u>et</u> <u>al</u>. (1991)<br /> <u>Mol.</u> <u>Gen.</u> <u>Genet.</u> 230, 17-24). The relative levels of these three holoenzyme<br /> forms changed depending on the phase of cell growth. In the <u>in</u> <u>vitro</u> mixed<br /> transcription assay using 33 different <u>E.</u> <u>coli</u> promoters, one of the<br /> stationary-phase RNA polymerase, S1, showed promoter recognition properties<br /> which are significantly different from that of holoenzyme from exponentially<br /> growing cells. <br />  Enzyme reconstitution experiments showed that the altered promoter<br /> selectivity is due to alteration in core enzyme. After a variety of attempts<br /> to achieve <u>in</u> <u>vitro</u> interconversion between the exponential and the stationary<br /> phase RNA polymerases, S1-form enzyme was found to be converted <u>in</u> <u>vitro</u> into<br /> such an enzyme as the log-phase form, following incubation with nucleotides or<br /> pyrophosphate (Ozaki, M. <u>et</u> <u>al</u>., (1991) <u>Nucleic</u> <u>Acids</u> <u>Res.</u> in press). The<br /> conversion was indicated by not only the shift of elution position from a<br /> phosphocellulose column but also the change in the promoter selectivity. Using<br /> polyphosphate kinase (PPK) which polymerizes the terminal phosphate of ATP to<br /> a long chain polyphosphate in a freely reversible reaction, polyphosphate was<br /> detected in the stationary-phase RNA polymerase (Ozakl, M. <u>et</u> <u>al</u>., in<br /> preparation). These results altogether lead to the possibility that RNA<br /> polymerase is converted into the stationary-phase form by binding<br /> polyphosphate. I propose that the modulation of RNA polymerase by<br /> polyphosphate plays a role in the global switch of gene transcription during<br /> the growth transition of <u>E.</u> <u>coli</u> to stationary phase.
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