| 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 |
|
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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
|
| フリガナ |
オザキ, ミワコ
|
| 著者 |
OZAKI, Miwako
|
| 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 |
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|
学位名 |
博士（理学） |
| 学位記番号 |
|
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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 |
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|
学位授与年月日 |
1992-03-16 |
| 学位授与年度 |
|
|
|
1991 |
| 要旨 |
|
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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. |
| 所蔵 |
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|
値 |
有 |
要旨・審査要旨 / Abstract, Screening Result (189.5 kB)
