NDLI: In Vivo Assay of Protein-Protein Interactions in Hin-Mediated DNA Inversion

Content Provider	PubMed Central
Author	Lee, Sun Young Lee, Hee Jung Lee, Heejin Kim, Shukho Cho, Eun Hee Lim, Heon Man
Copyright Year	1998
Abstract	In order to form the catalytic nucleoprotein complex called the invertasome in the Hin-mediated DNA inversion reaction, interactions of the DNA-binding proteins Hin and Fis are required. Assays for these protein-protein interactions have been exploited with protein cross-linkers in vitro. In this study, an in vivo assay system that probes protein-protein interactions was developed. The formation of a DNA loop generated by protein interactions resulted in transcriptional repression of an artificially designed operon, which in turn increased the chance of survival of Escherichia coli host cells in a streptomycin-containing medium. Using this system, we were able to assay the Hin-Hin interaction that results in the pairing of the two recombination sites and protein interactions that result in the formation of the invertasome. This assay system also led us to find that an individual Hin dimer bound on a recombination site can form a stable complex with Fis bound on the recombinational enhancer; this finding has never been observed in in vitro studies. Possible pathways toward the formation of the invertasome are discussed based on the assay results for a previously reported Hin mutant.
Starting Page	5954
File Format	PDF
ISSN	10985530
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	22
Volume Number	180
Language	English
Publisher	American Society for Microbiology
Publisher Date	1998-11-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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Hin-mediated Inversion on Positively Supercoiled DNA

Intermediates in Hin-mediated DNA inversion: a role for Fis and the recombinational enhancer in the strand exchange reaction.

Identification of two functional regions in Fis: the N-terminus is required to promote Hin-mediated DNA inversion but not lambda excision.

Phase variation and the Hin protein: in vivo activity measurements, protein overproduction, and purification.

In vivo identification of intermediate stages of the DNA inversion reaction catalyzed by the Salmonella Hin recombinase.

Hin Recombinase Mutants Functionally Disrupted in Interactions with Fis

Hin-mediated DNA knotting and recombining promote replicon dysfunction and mutation

Communication between Hin recombinase and Fis regulatory subunits during coordinate activation of Hin-catalyzed site-specific DNA inversion

Effect of DNA Superhelicity and Bound Proteins on Mechanistic Aspects of the Hin-Mediated and Fis-Enhanced Inversion

In Vivo Assay of Protein-Protein Interactions in Hin-Mediated DNA Inversion

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Hin-mediated Inversion on Positively Supercoiled DNA

Intermediates in Hin-mediated DNA inversion: a role for Fis and the recombinational enhancer in the strand exchange reaction.

Identification of two functional regions in Fis: the N-terminus is required to promote Hin-mediated DNA inversion but not lambda excision.

Phase variation and the Hin protein: in vivo activity measurements, protein overproduction, and purification.

In vivo identification of intermediate stages of the DNA inversion reaction catalyzed by the Salmonella Hin recombinase.

Hin Recombinase Mutants Functionally Disrupted in Interactions with Fis

Hin-mediated DNA knotting and recombining promote replicon dysfunction and mutation

Communication between Hin recombinase and Fis regulatory subunits during coordinate activation of Hin-catalyzed site-specific DNA inversion

Effect of DNA Superhelicity and Bound Proteins on Mechanistic Aspects of the Hin-Mediated and Fis-Enhanced Inversion

In Vivo Assay of Protein-Protein Interactions in Hin-Mediated DNA Inversion