東華大學圖書館 |

Language: English

Help

回圖書館首頁

手機版館藏查詢

Back

Switch To: Labeled | MARC Mode | ISBD

Suppression of LamB-LacZ hybrid jamm...

Hand, Nicholas Joseph.

Linked to FindBook

Google Book

Amazon

博客來

Suppression of LamB-LacZ hybrid jamming in Escherichia coli.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Suppression of LamB-LacZ hybrid jamming in Escherichia coli./
Author:	Hand, Nicholas Joseph.
Description:	253 p.
Notes:	Adviser: Thomas J. Silhavy.
Contained By:	Dissertation Abstracts International62-11B.
Subject:	Biology, Genetics. -
Online resource:	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.
LDR:02974nam 2200301 a 45 001 928230
005 20110426
008 110426s2002 eng d
020 $a 0493457461
035 $a (UnM)AAI3033018
035 $a AAI3033018
040 $a UnM $c UnM
100 1 $a Hand, Nicholas Joseph. $3 1251693
245 1 0 $a Suppression of LamB-LacZ hybrid jamming in Escherichia coli.
300 $a 253 p.
500 $a Adviser: Thomas J. Silhavy.
500 $a Source: Dissertation Abstracts International, Volume: 62-11, Section: B, page: 4944.
502 $a Thesis (Ph.D.)--Princeton University, 2002.
520 $a 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.
590 $a School code: 0181.
650 4 $a Biology, Genetics. $3 1017730
650 4 $a Biology, Molecular. $3 1017719
690 $a 0307
690 $a 0369
710 2 0 $a Princeton University. $3 645579
773 0 $t Dissertation Abstracts International $g 62-11B.
790 $a 0181
790 1 0 $a Silhavy, Thomas J., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3033018