The transactivation region of the Fis protein that controls site-specific DNA inversion contains extended mobile β-hairpin arms

The Fis protein regulates site‐specific DNA inversion catalyzed by a family of DNA invertases when bound to a cis‐acting recombinational enhancer. As is often found for transactivation domains, previous crystal structures have failed to resolve the conformation of the N‐terminal inversion activation...

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Bibliographic Details
Published in:The EMBO journal 1997-11, Vol.16 (22), p.6860-6873
Main Authors: Safo, Martin K., Yang, Wei-Zen, Corselli, Leah, Cramton, Sarah E., Yuan, Hanna S., Johnson, Reid C.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - metabolism
Computer Simulation
crystal structure
Crystallography, X-Ray
Cysteine - chemistry
DNA inversion
DNA Mutational Analysis
DNA Nucleotidyltransferases - metabolism
Factor For Inversion Stimulation Protein
Fis
Integration Host Factors
Models, Molecular
Molecular Sequence Data
Oxidation-Reduction
Protein Structure, Secondary
Recombination, Genetic
site-specific DNA recombination
Trans-Activators - chemistry
Trans-Activators - genetics
Trans-Activators - metabolism
transactivation
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Summary:The Fis protein regulates site‐specific DNA inversion catalyzed by a family of DNA invertases when bound to a cis‐acting recombinational enhancer. As is often found for transactivation domains, previous crystal structures have failed to resolve the conformation of the N‐terminal inversion activation region within the Fis dimer. A new crystal form of a mutant Fis protein now reveals that the activation region contains two β‐hairpin arms that protrude over 20 Å from the protein core. Saturation mutagenesis identified the regulatory and structurally important amino acids. The most critical activating residues are located near the tips of the β‐arms. Disulfide cross‐linking between the β‐arms demonstrated that they are highly flexible in solution and that efficient inversion activation can occur when the β‐arms are covalently linked together. The emerging picture for this regulatory motif is that contacts with the recombinase at the tip of the mobile β‐arms activate the DNA invertase in the context of an invertasome complex.
ISSN:0261-4189
1460-2075
1460-2075
DOI:10.1093/emboj/16.22.6860