Abstract
By analyzing specific protein-DNA interactions, molecular recognition processes can be better understood. How do distinct proteins recognize specific DNA sequences? Prokaryotic restriction endonucleases, for example, are characterized by highly specific DNA interactions and therefore are excellent models to study recognition events. More than 3,300 type II restriction endonucleases are known, recognizing about 200 distinct DNA specificities (Roberts and Macelis 2001). Among this large group of functionally related enzymes is a considerable number of isoschizomers, proteins isolated from different microbial species that interact with the same DNA sequence. However, there does not appear to be noteworthy homology in amino acid sequence among these enzymes (for a review see Pingoud and Jeltsch 2001). Did enzymes that interact with the same DNA sequence develop independent structures or mechanisms to interact with a specific target site? Are there any as yet unknown common rules of DNA recognition? To date, X-ray crystallography of protein-DNA complexes is without doubt the most informative method for understanding specific recognition. However, X-ray crystallography can be slow because obtaining good diffracting crystals is a very time-consuming and unpredictable process. Thus, faster methods are sought to increase the data pool on recognition complexes.
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References
Cornille F, Emery P, Schüler W, Lenoir C, Mach B, Roques BP, Reith W (1998) DNA-binding properties of a chemically synthesized DNA-binding domain of hRFX1. Nucleic Acids Res 26: 2143–2149
Jeltsch A, Alves J, Urbanke C, Maass G, Eckstein H, Lianshan Z, Bayer E, Pingoud A (1995) A dodecapeptide comprising the extended chain-a4 region of the restriction endonuclease EcoRI specifically binds to the EcoRI recognition site. J Biol Chem 270: 5122–5129
Pingoud A, Jeltsch A (2001) Structure and function of type II restriction endonucleases. Nucleic Acids Res 29: 3705–3727
Reuter M, Schneider-Mergener J, Kupper D, Meisel A, Mackeldanz P, Krüger DH, Schroeder C (1999) Regions of endonuclease EcoR11 involved in DNA target recognition identified by membrane-bound peptide repertoires. J Biol Chem 274: 5213–5221
Roberts RJ, Macelis D (2001) REBASE-restriction enzymes and methylases. Nucleic Acids Res 29: 268–269
Talanian RV, McKnight J, Kim PS (1990) Sequence-specific DNA-binding by a short peptide dimer. Science 249: 769–771
Talanian RV, McKnight J, Rutkowski R, Kim PS (1992) Minimum length of a sequence-specific DNA-binding peptide. Biochemistry 31: 6871–6875
Wang L, Voloshin ON, Stasiak A, Stasiak A, Camerini-Otero RD (1998) Homologous DNA pairing domain peptides of RecA protein: intrinsic propensity to form 13-structures and filaments. J Mol Biol 277: 1–11
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© 2002 Springer-Verlag Berlin Heidelberg
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Reuter, M., Möncke-Buchner, E. (2002). Analysis of Protein-DNA Interactions. In: Koch, J., Mahler, M. (eds) Peptide Arrays on Membrane Supports. Springer Lab Manuals. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-09229-3_7
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DOI: https://doi.org/10.1007/978-3-662-09229-3_7
Publisher Name: Springer, Berlin, Heidelberg
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