Abstract
In several processes related to gene expression and recombination, the DNA double helix has to be bent in a specific, well-defined topography to permit distant sites on DNA to approach each other or to facilitate interaction between proteins or protein and DNA sites that are located farther away along the DNA. The bending of DNA can be achieved either by certain base pair sequences (A-tracts) or, better, by DNA-binding proteins which stabilize a well-determined and specific DNA bend and, consequently, a specific DNA configuration (Travers 1991a,b).
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References
Biosym Technologies (1990) Discover user guide, Version 2.6.0. San Diego, CA
Brennan RG, Matthews BW (1989) The helix-turn-helix DNA binding motif. J Biol Chem 264: 1903–1906
Bruist MF, Glasgow AC, Johnson RC, Simon MI (1987) FIS binding to the recombinational enhancer of the Hin DNA inversion system. Genes Dev 1: 762–772
Choe HW, Labahn J, Itoh S, Koch C, Kahmann R, Saenger W (1989) Crystallization of the DNA binding Escherichia coli protein FIS. J Mol Biol 208: 209–210
Gille H, Egan JB, Roth A, Messer W (1991) The FIS protein binds and bends the origin of chromosomal DNA replication. oriC, of Escherichia coli. Nucleic Acids Res 19: 4167–4172
Haffter B, Bickle TA (1987) Purification and DNA binding properties of FIS and Cin, two proteins required for the bacteriophage PI site-specific recombination system, cin. J Mol Biol 198: 579–587
Heichmann KA, Johnson RC (1990) The Hin invertasome: protein-mediated joining of distant recombination sites at the enhancer. Science 249: 511–517
Hübner P, Arber W (1989) Mutational analysis of a prokaryotic recombinational enhancer element with two functions. EMBO J 8: 577–585
Johnson RC, Bruist MF, Simon MI (1986) Host protein requirements for in vitro site-specific recombination. Cell 46: 531–539
Johnson RC, Glasgow AC, Simon MI (1987) Spatial relationship of the FIS binding sites for Hin recombinational enhancer activity. Nature 329: 462–465
Johnson RC, Ball CA, Pfeffer D, Simon MI (1988) Isolation of the gene encoding the Hinrecombinational enhancer binding protein. Proc Natl Acad Sci USA 85: 3484–3488
Koch C (1988) Escherichia coli Faktor für sequenzspezifische DNA-Inversion: Charakterisierung des Proteins und Klonierung des Gens. PhD Thesis, Freie Universität Berlin
Koch C, Kahmann R (1986) Purification and properties of the Escherichia coli host factor required for inversion of the G segment in bacteriophage Mu. J Biol Chem 261: 15673–15678
Koch C, Ninnemann O, Fuss H, Kahmann R (1991) The N-terminal part of the E. coli DNA binding protein FIS is essential for stimulating site-specific DNA inversion but is not required for specific DNA binding. Nucleic Acids Res 19: 5915–5922
Kostrewa D, Granzin J, Koch C, Choe HW, Raghunathan S, Wolf W, Labahn J, Kahmann R, Saenger W (1991) Three-dimensional structure of the E. coli DNA- binding protein FIS. Nature 349: 178–180
Kostrewa D, Granzin J, Stock D, Choe HW, Labahn J, Saenger W (1992) Crystal structure of the factor for inversion stimulation (FIS) at 2.0 resolution. J Mol Biol 226: 209–226
Lavery R, Sklenar H (1989) Defining the structure of irregular nucleic acids: conventions and principles. J Biomol Struct Dynam 6: 655–667
Nilsson L, Vanet A, Vijgenboom E, Bosch L (1990) the role of FIS in trans activation of stable RNA operaters of E. coli. EMBO J 9: 727–734
Ninnemann O, Koch C, Kahmann R (1992) The E. coli fis promoter is subject to stringent control and autoregulation. EMBO J 11: 1075–1083
Osuna R, Finkel SE, Johnson RC (1991) Identification of two functional regions in FIS: the N-terminus is required to promote Hin-mediated DNA inversion but not X excision. EMBO J 10: 1593–1603
Pabo CO, Sauer RT (1984) Protein-DNA recognition. Annu Rev Biochem 53: 293–321
Ross W, Thompson JF, Newlands JT, Gourse RL (1990) E. coli FIS protein activates ribosomal RNA transcription in vitro and in vivo. EMBO J 9: 3733–3742
Sandmann C (1993) Structur des Komplexes zwischen DNA und Faktor für Inversions- Stimulierung (FIS): Modellbau-Studien und Elektronen-Mikroskopie. PhD Thesis, Freie Universität Berlin
Schultz SC, Shields GC, Steitz TA (1991) Crystal structure of a CAP-DNA complex: the DNA is bent by 90°. Science 253: 1001–1007
Steitz TA (1990) Structural studies of protein-nucleic acid interaction: the sources of sequence-specific binding. Q Rev Biophys 23: 205–280
Thompson JF, Landy A (1988) Empirical estimation for protein-induced DNA bending angles: applications to X site-specific recombination complexes. Nucleic Acids Res 16: 9687–9705
Thompson JF, de Vargas LM, Koch C, Kahmann R, Landy A (1987) Cellular factors couple recombination with growth phase: characterization of a new component in the X site-specific recombination pathway. Cell 50: 901–908
Travers AA (1991a) DNA bending and kinking. Curr Opinion Struct Biol 1: 114–122
Travers AA (1991b) To bend or… ? Curr Biol 1: 171–173
Yuan HS, Finkel SE, Feng JA, Kaczor-Grzeskowiak M, Johnson RC, Dickerson RE (1991) The molecular structure of wild-type and a mutant FIS protein: relationship between mutational changes and recombinational enhancer function or DNA binding. Proc Natl Acad Sci USA 88: 9558–9562
Zacharias M, Göringer HU, Wagner R (1992) Analysis of the FIS-dependent and FIS- independent transcription activation mechanism of the E. coli ribosomal RNA PI promoter. Biochemistry 31: 2621–2628
Zhurkin VB, Ulynaov NB, Gorin AA, Jernigan RL (1991) Static and statistical bending of DNA evaluated by Monte Carlo simulations. Proc Natl Acad Sci USA 88: 7046–7050
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Saenger, W. et al. (1993). Structural and Functional Aspects of the DNA Binding Protein FIS. In: Eckstein, F., Lilley, D.M.J. (eds) Nucleic Acids and Molecular Biology. Nucleic Acids and Molecular Biology, vol 7. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-77950-3_9
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DOI: https://doi.org/10.1007/978-3-642-77950-3_9
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