Three-dimensional structure of the E. coli DMA-binding protein FIS

@article{Kostrewa1991ThreedimensionalSO,
  title={Three-dimensional structure of the E. coli DMA-binding protein FIS},
  author={Dirk Kostrewa and Joachim Granzin and Christian Koch and Hui-Woog Choe and Srinivasan Raghunathan and Wojciech Wolf and J{\"o}rg Labahn and Regine Kahmann and Wolfram Saenger},
  journal={Nature},
  year={1991},
  volume={349},
  pages={178-180}
}
THE factor for inversion stimulation, FIS, is involved in several cellular processes, including site-specific recombination and tran-scriptional activation1–4. In the reactions catalysed by the DNA invertases Gin, Hin and Cin, FIS stimulates recombination by binding to an enhancer sequence1. Within the enhancer, two FIS dimers (each 2 x 98 amino acids)5–7 bind to two 15-base-pair consensus sequences8,9 (Fig. 1) and induce bending of DNA10,11. Current models propose that the enhancer–FIS complex… 
Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution.
The factor for inversion stimulation (FIS) binds as a homodimeric molecule to a loose 15 nucleotide consensus sequence in DNA. It stimulates DNA-related processes, such as DNA inversion and excision,
Biochemical identification of base and phosphate contacts between Fis and a high-affinity DNA binding site.
TLDR
Functional evidence is provided for some of the most critical interactions between Fis and DNA required for a high binding affinity and demonstrates the large contribution made by numerous phosphates to the stability of the Fis-DNA complex.
The molecular structure of wild-type and a mutant Fis protein: relationship between mutational changes and recombinational enhancer function or DNA binding.
TLDR
The proposed complex explains the experimentally observed patterns of methylation protection and DNase I cleavage hypersensitivity, and accounts for the effects of mutations in the Fis sequence.
Identification of the λ integrase surface that interacts with Xis reveals a residue that is also critical for Int dimer formation
  • D. Warren, M. D. Sam, +6 authors A. Landy
  • Biology, Medicine
    Proceedings of the National Academy of Sciences of the United States of America
  • 2003
TLDR
NMR titration data with a peptide corresponding to Xis residues 57–69 strongly suggest that the carboxyl-terminal tail of Xis and the α-helix of the aminoterminal domain of Int comprise the primary interaction surface for these two proteins.
The Fis protein: it's not just for DNA inversion anymore
TLDR
The X-ray crystal structure of Fis has been determined and insights into its mode of DNA binding and mechanisms of action in these disparate systems are being made.
Genetic and biochemical analysis of the synaptic complex of invertase Gin.
The Gin inversion system of bacteriophage Mu requires the formation of a synaptic complex of unique topology, where the two Gin dimers bound at the recombination gix sites are interacting to form an
Stimulation of DNA inversion by FIS: evidence for enhancer-independent contacts with the Gin-gix complex.
TLDR
It is demonstrated that FIS mutants impaired in DNA binding are capable of either positively or negatively affecting the inversion reaction both in vivo and in vitro and suggest that F IS plays a dual role in the inversions reaction and stimulates both the assembly of the synaptic complex as well as DNA strand cleavage.
Mechanism of chromosome compaction and looping by the Escherichia coli nucleoid protein Fis.
TLDR
Results suggest that Fis may play a role in vivo as a domain barrier element by organizing DNA loops within the E. coli chromosome through Fis-mediated DNA looping.
Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions.
The structure of the 52-amino acid DNA-binding domain of the prokaryotic Hin recombinase, complexed with a DNA recombination half-site, has been solved by x-ray crystallography at 2.3 angstrom
Crystal structure of the nucleoid-associated protein Fis (PA4853) from Pseudomonas aeruginosa.
TLDR
The crystal structure of PaFis, which is composed of a four-helix bundle and forms a homodimer, is reported and structure-based mutagenesis revealed that several conserved basic residues in the HTH motif play essential roles in DNA binding.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 25 REFERENCES
Structure of Arc represser in solution: evidence for a family of β-sheet DMA-binding proteins
TLDR
The three-dimensional structure of the Arc dimer is determined from an extensive set of inter proton-distance data obtained from 1H NMR spectroscopy, and two Arc dimers bind with their β-sheet regions in successive major grooves on one side of the DNA helix, similar to the Met repressor interaction.
Crystallization of the DNA-binding Escherichia coli protein FIS.
The specific DNA-binding protein FIS (factor for inversion stimulation), which stimulates site-specific DNA inversion by interaction with an enhancer sequence, was purified from an Escherichia coli
Gin-mediated DNA inversion: product structure and the mechanism of strand exchange.
TLDR
A quantitative model for the mechanism of Gin recombination is constructed that includes the distribution of supercoils in the synaptic complex, their alteration by strand exchange, and specific roles for the two proteins needed for recombination.
The role of FIS in trans activation of stable RNA operons of E. coli.
TLDR
It is demonstrated that the E.coli protein FIS (Factor for Inversion Stimulation) also binds to the UAS of the thrU(tufB) operon forming three protein‐DNA complexes, suggesting that transcription of the three operons, if not of more stable RNA operon, is activated by a common trans activator.
The helix-turn-helix DNA binding motif.
TLDR
The role of the heliiturn-helix in recognition of sequence-specific binding sites on DNA will be evaluated in light of the recently defined repressor-operator complexes.
Structure of the cro repressor from bacteriophage λ and its interaction with DNA
TLDR
The three-dimensional structure of the 66-amino acid cro repressor protein of bacteriophage λ suggests how it binds to its operator DNA and suggests a pair of 2-fold-related α-helices of the represser seem to be a major determinant in recognition and binding.
Bent DNA is needed for recombinational enhancer activity in the site-specific recombination system Cin of bacteriophage P1. The role of FIS protein.
TLDR
DNA bending assays identify this requirement as a change of the enhancer DNA conformation, which FIS protein is able to induce and to stabilize, which can be blocked by mutations in the central segment between the two FIS binding sites of the Hin enhancer.
Cellular factors couple recombination with growth phase: Characterization of a new component in the λ site-specific recombination pathway
TLDR
FIS (factor for inversion stimulation), a new cellular component of the lambda site-specific recombination pathway, binds to a specific region in the lambda attP overlapping the Xis binding sites and can bind cooperatively with Xis to these sites.
Mutational analysis of a prokaryotic recombinational enhancer element with two functions.
TLDR
These sequences appear to be highly evolved allowing only a few mutations without affecting either of the biological functions, in line with the orientation independence of enhancer action with respect to the crossing‐over sites.
Fis binding to the recombinational enhancer of the Hin DNA inversion system.
TLDR
Results support a model for the role of the recombinational enhancer in Hin-mediated inversion in which the interaction between Hin bound at recombination sites and Fis bound to each domain of the rejoining enhancer results in a structure with the proper alignment and topology to promote DNA inversion.
...
1
2
3
...