國立高雄大學圖資館 |

Language: English

Back

Molecular biology of anaerobic toluene and m-xylene oxidation in Azoarcus sp. strain T.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Molecular biology of anaerobic toluene and m-xylene oxidation in Azoarcus sp. strain T.
Author:	Achong, Gypsy Rebekah.
Description:	92 p.
Notes:	Adviser: Alfred M. Spormann.
Notes:	Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4545.
Contained By:	Dissertation Abstracts International64-09B.
Subject:	Engineering, Environmental.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3104185
ISBN:	0496517538

Molecular biology of anaerobic toluene and m-xylene oxidation in Azoarcus sp. strain T.
Achong, Gypsy Rebekah.

Molecular biology of anaerobic toluene and m-xylene oxidation in Azoarcus sp. strain T. [electronic resource] - 92 p.

Adviser: Alfred M. Spormann.

Thesis (Ph.D.)--Stanford University, 2003.

Azoarcus sp. strain T is a facultative denitrifying bacterium that anaerobically mineralizes both toluene and m-xylene. To facilitate genetic studies in this microorganism, a reliable transformation procedure was developed. Several broad host range vectors that are replicated in Azoarcus sp. strain T were identified, as well as a suicide vector system that allowed construction of chromosomal insertions and deletions.

ISBN: 0496517538Subjects--Topical Terms:

212478
Engineering, Environmental.

Molecular biology of anaerobic toluene and m-xylene oxidation in Azoarcus sp. strain T.
LDR:03427nmm _2200289 _450 001 162158
005 20051017073416.5
008 230606s2003 eng d
020 $a 0496517538
035 $a 00148659
035 $a 162158
040 $a UnM $c UnM
100 0 $a Achong, Gypsy Rebekah. $3 227274
245 1 0 $a Molecular biology of anaerobic toluene and m-xylene oxidation in Azoarcus sp. strain T. $h [electronic resource]
300 $a 92 p.
500 $a Adviser: Alfred M. Spormann.
500 $a Source: Dissertation Abstracts International, Volume: 64-09, Section: B, page: 4545.
502 $a Thesis (Ph.D.)--Stanford University, 2003.
520 # $a Azoarcus sp. strain T is a facultative denitrifying bacterium that anaerobically mineralizes both toluene and m-xylene. To facilitate genetic studies in this microorganism, a reliable transformation procedure was developed. Several broad host range vectors that are replicated in Azoarcus sp. strain T were identified, as well as a suicide vector system that allowed construction of chromosomal insertions and deletions.
520 # $a Natural attenuation is a promising technology for remediation of gasoline-contaminated sites. Understanding the biochemistry and molecular biology of enzymes responsible for natural attenuation will improve our ability to predict and enhance natural attenuation. Biochemical studies revealed a novel fumarate addition reaction for initiation of anaerobic toluene oxidation. This reaction appears to be a common mode for initiation of anaerobic mineralization of a wide range of compounds. The molecular biology of anaerobic toluene and m-xylene oxidation in Azoarcus sp. strain T will be discussed in this work.
520 # $a The first step of the pathway for anaerobic oxidation of toluene, catalyzed by benzylsuccinate synthase, is the addition of toluene to fumarate to form benzylsuccinate. The genes encoding the three subunits of benzylsuccinate synthase were cloned and sequenced. Analysis of a null mutant in the gene encoding the largest subunit of benzylsuccinate synthase, bssA, showed that a single enzyme, benzylsuccinate synthase, is necessary for growth on both toluene and m-xylene. Reverse transcriptase-PCR studies, as well as Northern blot studies and transcriptional start site mapping, showed that the structural genes encoding benzylsuccinate synthase, bssCAB , as well as two other genes, named bssD and bssE, are transcribed as an operon. Transcriptional start sites were defined for the bssDCABE operon, as well as for an upstream operon containing two genes, tdiS and tdiR. To quantitatively determine bssDCABE expression under different conditions, a translational lacZ fusion to bssB was generated.
520 # $a tdiS encodes a protein with homology to sensor kinases of two-component regulatory systems. A null mutant in the tdiS gene was constructed to determine its role in anaerobic toluene oxidation. The tdiS gene was heterologously expressed in Escherichia coli, and polyclonal antibodies to inclusion bodies of the TdiS protein were generated for analysis of expression of tdiS.
590 $a School code: 0212.
650 # 0 $a Engineering, Environmental. $3 212478
650 # 0 $a Biology, Microbiology. $3 226920
710 0 # $a Stanford University. $3 212607
773 0 # $g 64-09B. $t Dissertation Abstracts International
790 $a 0212
790 1 0 $a Spormann, Alfred M., $e advisor
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://libsw.nuk.edu.tw/login?url=http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3104185 $z http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3104185