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Characterization of plasmid-encoded ...

Gunton, James Eric.

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Characterization of plasmid-encoded proteins that mediate or inhibit R27 conjugative transfer.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Characterization of plasmid-encoded proteins that mediate or inhibit R27 conjugative transfer./
Author:	Gunton, James Eric.
Description:	198 p.
Notes:	Source: Dissertation Abstracts International, Volume: 67-04, Section: B, page: 1811.
Contained By:	Dissertation Abstracts International67-04B.
Subject:	Biology, Microbiology. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=NR13980
ISBN:	9780494139806

Characterization of plasmid-encoded proteins that mediate or inhibit R27 conjugative transfer.
Gunton, James Eric.

Characterization of plasmid-encoded proteins that mediate or inhibit R27 conjugative transfer. - 198 p.

Source: Dissertation Abstracts International, Volume: 67-04, Section: B, page: 1811.

Thesis (Ph.D.)--University of Alberta (Canada), 2006.

Bacterial conjugation is a mechanism of horizontal gene transfer that requires the intimate association of donor and recipient cells. There are three multiprotein complexes which mediate the transfer of plasmid DNA into neighbouring bacteria: a membrane-spanning Mpf complex, the cytoplasmic-associated relaxosome and a hexameric coupling protein. The link between the Mpf complex and the relaxosome is provided by the coupling protein. An interaction between the IncHI1 plasmid R27 Mpf complex and coupling protein has been previously identified through bacterial two-hybrid and immunoprecipitation studies. Using these techniques, an interaction was detected between the R27 coupling protein TraG and TraJ, an essential conjugative protein that was originally classified as a relaxosome component. A module encoding TraG and TraJ has been found to be co-inherited in a number of plasmid and chromosomal genomes. Homologues of TraG and TraJ from a variety of these genomic sources were found to interact. Furthermore, limited homology has been identified between the transmembrane and nucleotide binding domains of the SpoIIIE/FtsK family of DNA translocases and TraJ and TraG, respectively. TraJ has been reclassified as an accessory protein to the R27 coupling protein TraG.

ISBN: 9780494139806Subjects--Topical Terms:

1017734
Biology, Microbiology.

Characterization of plasmid-encoded proteins that mediate or inhibit R27 conjugative transfer.
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020 $a 9780494139806
035 $a (UMI)AAINR13980
035 $a AAINR13980
040 $a UMI $c UMI
100 1 $a Gunton, James Eric. $3 1281931
245 1 0 $a Characterization of plasmid-encoded proteins that mediate or inhibit R27 conjugative transfer.
300 $a 198 p.
500 $a Source: Dissertation Abstracts International, Volume: 67-04, Section: B, page: 1811.
502 $a Thesis (Ph.D.)--University of Alberta (Canada), 2006.
520 $a Bacterial conjugation is a mechanism of horizontal gene transfer that requires the intimate association of donor and recipient cells. There are three multiprotein complexes which mediate the transfer of plasmid DNA into neighbouring bacteria: a membrane-spanning Mpf complex, the cytoplasmic-associated relaxosome and a hexameric coupling protein. The link between the Mpf complex and the relaxosome is provided by the coupling protein. An interaction between the IncHI1 plasmid R27 Mpf complex and coupling protein has been previously identified through bacterial two-hybrid and immunoprecipitation studies. Using these techniques, an interaction was detected between the R27 coupling protein TraG and TraJ, an essential conjugative protein that was originally classified as a relaxosome component. A module encoding TraG and TraJ has been found to be co-inherited in a number of plasmid and chromosomal genomes. Homologues of TraG and TraJ from a variety of these genomic sources were found to interact. Furthermore, limited homology has been identified between the transmembrane and nucleotide binding domains of the SpoIIIE/FtsK family of DNA translocases and TraJ and TraG, respectively. TraJ has been reclassified as an accessory protein to the R27 coupling protein TraG.
520 $a Site specific mutagenesis and immunofluorescent (IMF) microscopic studies on the R27 coupling protein have identified functional domains and cellular localization of this conjugative protein. Essential residues of TraG within the nucleotide binding domain were determined and the periplasmic domain of the coupling protein was found to mediate an interaction with the Mpf protein TrhB. The R27 coupling protein was visualized within discrete, membrane-associated foci using IMF microscopy. The number and position of these foci were comparable to the fluorescent foci produced by the GFP-labeled R27 Mpf complex.
520 $a The R27 proteins EexH and TrhZ have been found to prevent the redundant transfer of IncH plasmid into recipient cells harbouring the isogenic or closely-related IncH plasmids. The two R27 Entry exclusion proteins EexH and TrhZ were determined to localize to the outer and inner membrane, respectively. Mutational analyses of the R27 exclusion genes have indicated that a functional exclusion protein is required in the donor cell to elicit an exclusion process. In conclusion, this thesis has characterized proteins which mediate or inhibit R27 conjugative transfer.
590 $a School code: 0351.
650 4 $a Biology, Microbiology. $3 1017734
650 4 $a Health Sciences, Immunology. $3 1017716
690 $a 0410
690 $a 0982
710 2 0 $a University of Alberta (Canada). $3 626651
773 0 $t Dissertation Abstracts International $g 67-04B.
790 $a 0351
791 $a Ph.D.
792 $a 2006
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=NR13980