Functional replacement of a protein-induced bend in a DNA recombination site.
In recent years the capacity of proteins to bend DNA by binding to specific sites has become a widely appreciated phenomenon. In many cases, the protein-DNA interaction is known to be functionally significant because destruction of the DNA site or the protein itself results in an altered phenotype. An important question to be answered in these cases is whether bending of DNA is important per se or is merely a consequence of the way a particular protein binds to DNA. Here we report direct evidence from the bacteriophage lambda integration system that a bend introduced by a protein is intrinsically important. We find that a binding site for a specific recombination protein known to bend DNA can be successfully replaced by two other modules that also bend DNA; related modules that fail to bend DNA are ineffective.
Goodman
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SD
Laboratory of Molecular Biology, National Institute of Mental Health, Bethesda, Maryland 20892.
Nash
H A
HA
D001426:Bacterial Proteins / Q000502:physiology; D010582:Bacteriophage lambda / Q000235:genetics*; D001665:Binding Sites; D004252:DNA Mutational Analysis; D004254:DNA Nucleotidyltransferases / Q000502:physiology; D004269:DNA, Bacterial / Q000235:genetics* / Q000648:ultrastructure; D004279:DNA, Viral / Q000235:genetics* / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000502:physiology*; D019426:Integrases; D034982:Integration Host Factors; D009690:Nucleic Acid Conformation; D011953:Receptors, Cyclic AMP / Q000502:physiology; D011995:Recombination, Genetic; D012045:Regulatory Sequences, Nucleic Acid
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D034982:Integration Host Factors; D011953:Receptors, Cyclic AMP; D004254:DNA Nucleotidyltransferases; D019426:Integrases