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Structure-Function Studies of Bacteriophage P2 Integrase and Cox protein
Stockholm University, Faculty of Science, Department of Genetics, Microbiology and Toxicology.
2005 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Probably no group of organisms has been as important as bacteriophages when it comes to the understanding of fundamental biological processes like transcriptional control, DNA replication, site-specific recombination, e.t.c.

The work presented in this thesis is a contribution towards the complete understanding of these organisms. Two proteins, integrase, and Cox, which are important for the choice of the life mode of bacteriophage P2, are investigated. P2 is a temperate phage, i.e. it can either insert its DNA into the host chromosome (by site-specific recombination) and wait (lysogeny), or it can produce new progeny with the help of the host protein machinery and thereafter lyse the cell (lytic cycle). The integrase protein is necessary for the integration and excision of the phage genome. The Cox protein is involved as a directional factor in the site-specific recombination, where it stimulates excision and inhibits integration. It has been shown that the Cox protein also is important for the choice of the lytic cycle. The choice of life mode is regulated on a transcriptional level, where two mutually exclusive promoters direct whether the lytic cycle (Pe) or lysogeny (Pc) is chosen. The Cox pro-tein has been shown to repress the Pc promoter and thereby making tran-scription from the Pe promoter possible, leading to the lytic cycle. Further, the Cox protein can function as a transcriptional activator on the parasite phage, P4. P4 has gained the ability to adopt the P2 protein machinery to its own purposes.

In this work the importance of the native size for biologically active integrase and Cox proteins has been determined. Further, structure-function analyses of the two proteins have been performed with focus on the protein-protein interfaces. In addition it is shown that P2 Cox and the P2 relative Wphi Cox changes the DNA topology upon specific binding. From the obtained results a mechanism for P2 Cox-DNA interaction is discussed.

The results from this thesis can be used in the development of a gene delivery system based on the P2 site-specific recombination system.

Place, publisher, year, edition, pages
Stockholm: Institutionen för genetik, mikrobiologi och toxikologi , 2005. , 145 p.
Keyword [en]
Bacteriophage P2, site-specific recombination, integrase, transcriptional switch
National Category
Genetics
Identifiers
URN: urn:nbn:se:su:diva-683ISBN: 91-7155-128-X (print)OAI: oai:DiVA.org:su-683DiVA: diva2:197142
Public defence
2005-10-31, Nordenskiöldsalen, Geovetenskapens hus, Svante Arrhenius väg 8 C, Stockholm, 13:00
Opponent
Supervisors
Available from: 2005-10-03 Created: 2005-10-03Bibliographically approved
List of papers
1. The multifunctional bacteriophage Cox protein requires oligomerization for biological activity
Open this publication in new window or tab >>The multifunctional bacteriophage Cox protein requires oligomerization for biological activity
2000 In: Journal of Bacteriology, ISSN 0021-9193, Vol. 182, no 23, 6714-6723 p.Article in journal (Refereed) Published
Identifiers
urn:nbn:se:su:diva-24272 (URN)
Note
Part of urn:nbn:se:su:diva-683Available from: 2005-10-03 Created: 2005-10-03Bibliographically approved
2. A comparative analysis of the multifunctional Cox proteins of the two heteroimmune phages P2 and Wphi
Open this publication in new window or tab >>A comparative analysis of the multifunctional Cox proteins of the two heteroimmune phages P2 and Wphi
Manuscript (Other academic)
Identifiers
urn:nbn:se:su:diva-24273 (URN)
Note
Part of urn:nbn:se:su:diva-683Available from: 2005-10-03 Created: 2005-10-03 Last updated: 2010-01-13Bibliographically approved
3. Dimerization of bacteriophage P2 integrase is not required for binding to its DNA target but for its biological activity
Open this publication in new window or tab >>Dimerization of bacteriophage P2 integrase is not required for binding to its DNA target but for its biological activity
2005 In: Gene, ISSN 0378-1119, Vol. 344, 221-231 p.Article in journal (Refereed) Published
Identifiers
urn:nbn:se:su:diva-24274 (URN)
Note
Part of urn:nbn:se:su:diva-683Available from: 2005-10-03 Created: 2005-10-03Bibliographically approved

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