Bacterial cytochromes P450-Studies on Cytochrome P450 102A2 and P450 102A3 of Bacillus subtilis
(2000)- Abstract
- Cytochromes P450 constitute a super-family of heme containing mixed function mono-oxygenases that is found in all branches of life. They introduce single oxygen atoms, mostly in the form of hydroxyl groups, into lipophilic substances and thereby render them more hydrophilic and susceptible to further reactions. Little is known about the bacterial cytochromes P450. I have in my thesis given an overview of the bacterial cytochromes P450 with emphasis on the Bacillus subtilis P450s that have been the subject of my Ph.D. studies. B. subtilis is the most well-studied bacterium next to Escherichia coli and is a model-organism for the Gram-positive bacteria. There are eight cytochromes P450 in B. subtilis strain 168 of which three have been the... (More)
- Cytochromes P450 constitute a super-family of heme containing mixed function mono-oxygenases that is found in all branches of life. They introduce single oxygen atoms, mostly in the form of hydroxyl groups, into lipophilic substances and thereby render them more hydrophilic and susceptible to further reactions. Little is known about the bacterial cytochromes P450. I have in my thesis given an overview of the bacterial cytochromes P450 with emphasis on the Bacillus subtilis P450s that have been the subject of my Ph.D. studies. B. subtilis is the most well-studied bacterium next to Escherichia coli and is a model-organism for the Gram-positive bacteria. There are eight cytochromes P450 in B. subtilis strain 168 of which three have been the subject of my research. The function of cytochrome P450 107J1 (Cyp107J1) is not known. Cyp102A2 and Cyp102A3 are fatty acid hydroxylases that show preferences for long-chain unsaturated and branched-chain fatty acids. The gene for Cyp102A3 is preceded by and lies in an operon with the gene for a fatty acid displaced transcriptional repressor, FatR. FatR binds and is displaced from its operator by unsaturated and branched-chain fatty acids, thereby allowing transcription. The cyp102A2 and fatR-cyp102A3 operons are expressed in the stationary phase and are controlled by the global transcriptional regulators Spo0A and AbrB, involving a novel B. subtilis pheromone. When studying Cyp107J1 a novel mode of resistance against the toxic leucine analogue, 4-azaleucine, was found. The resistance phenotype is due to a loss of function mutation in a transcriptional repressor, with the concomitant over-production of two membrane proteins. (Less)
- Abstract (Swedish)
- Popular Abstract in Swedish
Cytokrom P450 är en grupp enzymer som introducerar alkoholgrupper i främst icke-vattenlösliga ämnen. Alkoholgupperna gör dessa föreningar mer vattenlösliga och känsliga för fortsatta reaktioner. Cytokrom P450-enzymer återfinns i de tre domäner allt levande kan indelas i: eukaryoter (djur, växter, svampar, protozoer m.m.), bakterier och arkeér (ett slags bakterier som skiljer sig väsentligt från vanliga bakterier). Hos oss människor fungerar olika cytokrom P450 till exempel vid nedbrytning av gifter i levern, metabolism av kolesterol, hormoner och vitamin D. Cytokrom P450 i bakterier är ett område om vilket lite är känt. Bakteriella cytokrom P450 är till exempel inblandade i utnyttjandet av... (More) - Popular Abstract in Swedish
Cytokrom P450 är en grupp enzymer som introducerar alkoholgrupper i främst icke-vattenlösliga ämnen. Alkoholgupperna gör dessa föreningar mer vattenlösliga och känsliga för fortsatta reaktioner. Cytokrom P450-enzymer återfinns i de tre domäner allt levande kan indelas i: eukaryoter (djur, växter, svampar, protozoer m.m.), bakterier och arkeér (ett slags bakterier som skiljer sig väsentligt från vanliga bakterier). Hos oss människor fungerar olika cytokrom P450 till exempel vid nedbrytning av gifter i levern, metabolism av kolesterol, hormoner och vitamin D. Cytokrom P450 i bakterier är ett område om vilket lite är känt. Bakteriella cytokrom P450 är till exempel inblandade i utnyttjandet av ovanliga kolkällor och i syntes av antibiotika. Jag har i min avhandling sammanfattat vad som är kännt om cytokrom P450 i bakterier och i bakterien Bacillus subtilis i synnerhet. Jordbakterien B. subtilis är en modell-organism för de Gram-positiva bakterierna och den mest välstuderade bakterien efter tarmbakterien Escherichia coli. En av de intressanta saker jag fann under mina studier var en signalsubstans som styr uttrycket av två cytokrom P450 i B. subtilis. Denna substans verkar reglera ett flertal gener som är viktiga vid svältresponser hos B. subtilis. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/40780
- author
- Gustafsson, Mattias LU
- supervisor
- opponent
-
- Dr Saxild, Hans Henrik, Department of Microbiology, Technical University of Denmark, Lyngby, Denmark
- organization
- publishing date
- 2000
- type
- Thesis
- publication status
- published
- subject
- keywords
- Microbiology, AbrB, Spo0A, monooxygenase, heme, Bacillus subtilis, Cytochrome P450, bacteriology, virology, mycology, Mikrobiologi, bakteriologi, virologi, mykologi
- pages
- 174 pages
- publisher
- Department of Microbiology, Lund University
- defense location
- Rune Grubb hall, BMC, Sölvegatan 21, Lund
- defense date
- 2000-09-29 10:00:00
- external identifiers
-
- other:ISRN: LUNBDS/NBNB-1037/1-56 (2000)
- ISBN
- 91-7874-082-7
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Biology building (Closed 2011) (011008000), Division of Medical Microbiology (013250400)
- id
- bb85e134-1d17-490f-8665-4b182904b390 (old id 40780)
- date added to LUP
- 2016-04-04 10:47:12
- date last changed
- 2018-11-21 21:00:46
@phdthesis{bb85e134-1d17-490f-8665-4b182904b390,
abstract = {{Cytochromes P450 constitute a super-family of heme containing mixed function mono-oxygenases that is found in all branches of life. They introduce single oxygen atoms, mostly in the form of hydroxyl groups, into lipophilic substances and thereby render them more hydrophilic and susceptible to further reactions. Little is known about the bacterial cytochromes P450. I have in my thesis given an overview of the bacterial cytochromes P450 with emphasis on the Bacillus subtilis P450s that have been the subject of my Ph.D. studies. B. subtilis is the most well-studied bacterium next to Escherichia coli and is a model-organism for the Gram-positive bacteria. There are eight cytochromes P450 in B. subtilis strain 168 of which three have been the subject of my research. The function of cytochrome P450 107J1 (Cyp107J1) is not known. Cyp102A2 and Cyp102A3 are fatty acid hydroxylases that show preferences for long-chain unsaturated and branched-chain fatty acids. The gene for Cyp102A3 is preceded by and lies in an operon with the gene for a fatty acid displaced transcriptional repressor, FatR. FatR binds and is displaced from its operator by unsaturated and branched-chain fatty acids, thereby allowing transcription. The cyp102A2 and fatR-cyp102A3 operons are expressed in the stationary phase and are controlled by the global transcriptional regulators Spo0A and AbrB, involving a novel B. subtilis pheromone. When studying Cyp107J1 a novel mode of resistance against the toxic leucine analogue, 4-azaleucine, was found. The resistance phenotype is due to a loss of function mutation in a transcriptional repressor, with the concomitant over-production of two membrane proteins.}},
author = {{Gustafsson, Mattias}},
isbn = {{91-7874-082-7}},
keywords = {{Microbiology; AbrB; Spo0A; monooxygenase; heme; Bacillus subtilis; Cytochrome P450; bacteriology; virology; mycology; Mikrobiologi; bakteriologi; virologi; mykologi}},
language = {{eng}},
publisher = {{Department of Microbiology, Lund University}},
school = {{Lund University}},
title = {{Bacterial cytochromes P450-Studies on Cytochrome P450 102A2 and P450 102A3 of Bacillus subtilis}},
year = {{2000}},
}