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The topology of the Phd-Doc repressi...
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The University of Alabama in Huntsville.
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The topology of the Phd-Doc repressive complex.
Record Type:
Language materials, printed : Monograph/item
Title/Author:
The topology of the Phd-Doc repressive complex./
Author:
Hung, Sheng-Tien.
Description:
147 p.
Notes:
Adviser: Roy D. Magnuson.
Contained By:
Masters Abstracts International46-01.
Subject:
Biology, Microbiology. -
Online resource:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1445434
ISBN:
9780549129363
The topology of the Phd-Doc repressive complex.
Hung, Sheng-Tien.
The topology of the Phd-Doc repressive complex.
- 147 p.
Adviser: Roy D. Magnuson.
Thesis (M.S.)--The University of Alabama in Huntsville, 2007.
Transcription of the bacteriophage P1 addiction operon is negatively regulated by its products, Phd and Doc. In the repressive complex, two monomers of Doc bridge two dimers of Phd which in turn bind to two palindromic DNA sites within the operator. Each molecule of Phd can interact with Doc in two distinct ways; thus many different arrangements of Phd and Doc are possible. Here, the topology of the repressive complex was investigated using an oriented heterodimer approach. Chimeric operators and PhdR7S, a mutation that alters the DNA binding specificity of Phd, were used to put mutations with defects in one (PhdL59A) or both (PhdDelta(55-73)) of the interactions with Doc at specific positions within the repressive complex. Reciprocal experiments show that Doc interacts only with the outer two monomers of Phd in the repressive complex.
ISBN: 9780549129363Subjects--Topical Terms:
1017734
Biology, Microbiology.
The topology of the Phd-Doc repressive complex.
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147 p.
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Adviser: Roy D. Magnuson.
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Source: Masters Abstracts International, Volume: 46-01, page: 0268.
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Thesis (M.S.)--The University of Alabama in Huntsville, 2007.
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Transcription of the bacteriophage P1 addiction operon is negatively regulated by its products, Phd and Doc. In the repressive complex, two monomers of Doc bridge two dimers of Phd which in turn bind to two palindromic DNA sites within the operator. Each molecule of Phd can interact with Doc in two distinct ways; thus many different arrangements of Phd and Doc are possible. Here, the topology of the repressive complex was investigated using an oriented heterodimer approach. Chimeric operators and PhdR7S, a mutation that alters the DNA binding specificity of Phd, were used to put mutations with defects in one (PhdL59A) or both (PhdDelta(55-73)) of the interactions with Doc at specific positions within the repressive complex. Reciprocal experiments show that Doc interacts only with the outer two monomers of Phd in the repressive complex.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=1445434
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