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Suppression of LamB-LacZ hybrid jamm...
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Hand, Nicholas Joseph.
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Suppression of LamB-LacZ hybrid jamming in Escherichia coli.
紀錄類型:
書目-語言資料,印刷品 : Monograph/item
正題名/作者:
Suppression of LamB-LacZ hybrid jamming in Escherichia coli./
作者:
Hand, Nicholas Joseph.
面頁冊數:
253 p.
附註:
Adviser: Thomas J. Silhavy.
Contained By:
Dissertation Abstracts International62-11B.
標題:
Biology, Genetics. -
電子資源:
http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3033018
ISBN:
0493457461
Suppression of LamB-LacZ hybrid jamming in Escherichia coli.
Hand, Nicholas Joseph.
Suppression of LamB-LacZ hybrid jamming in Escherichia coli.
- 253 p.
Adviser: Thomas J. Silhavy.
Thesis (Ph.D.)--Princeton University, 2002.
The initial goal of the work presented here was to elucidate the mechanism of action of the elusive <italic>prlF1</italic> suppressor. The <italic>prlF1 </italic> mutation was isolated as a suppressor of the toxicity of the hybrid protein, LamB-LacZ Hyb42-1, which causes a general, lethal, protein export defect, termed hybrid jamming, when its expression is induced. Mutations in the same gene were identified independently as suppressors of the temperature sensitive requirement for the periplasmic protease DegP (HtrA). Thus, <italic> prlF1</italic> links two fields of long-standing interest: protein export, and envelope stress.
ISBN: 0493457461Subjects--Topical Terms:
1017730
Biology, Genetics.
Suppression of LamB-LacZ hybrid jamming in Escherichia coli.
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Source: Dissertation Abstracts International, Volume: 62-11, Section: B, page: 4944.
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Thesis (Ph.D.)--Princeton University, 2002.
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The initial goal of the work presented here was to elucidate the mechanism of action of the elusive <italic>prlF1</italic> suppressor. The <italic>prlF1 </italic> mutation was isolated as a suppressor of the toxicity of the hybrid protein, LamB-LacZ Hyb42-1, which causes a general, lethal, protein export defect, termed hybrid jamming, when its expression is induced. Mutations in the same gene were identified independently as suppressors of the temperature sensitive requirement for the periplasmic protease DegP (HtrA). Thus, <italic> prlF1</italic> links two fields of long-standing interest: protein export, and envelope stress.
520
$a
We knew from previous work that the <italic>prlF1</italic> mutation activates the cytoplasmic protease Lon, and that a wildtype copy of the ton gene was required for all the phenotypes of <italic>prlF1</italic>. What was not clear was the nature of the interaction of the two genes, nor indeed what function the Lon protease served in the process, since there is no detectable increase in the proteolysis of the hybrid in <italic>prlF1</italic> strains.
520
$a
The work presented here falls broadly into two section. The first half describes a directed mutagenesis approach, which has clarified the recessive nature of the <italic>prlF1</italic> suppressor, and which has led to believe that the mutant PrlF1 protein interacts directly with Lon. In the second half, I present the results of a screen for mutations that suppress the requirement for Ion, and in particular, the characterization of the <italic> ygdP</italic> gene. Two independent insertions in <italic>ygdP</italic>, which encodes a dinucleotide oligophosphate hydrolase, revela a novel mechanism of phenocopying <italic>prlF1</italic>. We propose two alternative models to explain the suppression of hybrid jamming by the loss of <italic>ygdP</italic> function. The remarkable commonality of the <italic>prlF1</italic> and <italic> ygdP</italic> phenotypes suggests a fundamental link between protein export defects, and the requirement for <italic>degP</italic> at high temperatures.
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http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3033018
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