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Steven D. Goodman Nerissa J. Velten Qian Gao Scott Robinson Anca M. Segall 《Journal of bacteriology》1999,181(10):3246-3255
Integration host factor (IHF) is a bacterial protein that binds and severely bends a specific DNA target. IHF binding sites are approximately 30 to 35 bp long and are apparently divided into two domains. While the 3' domain is conserved, the 5' domain is degenerate but is typically AT rich. As a result of physical constraints that IHF must impose on DNA in order to bind, it is believed that this 5' domain must possess structural characteristics conducive for both binding and bending with little regard for specific contacts between the protein and the DNA. We have examined the sequence requirements of the 5' binding domain of the IHF binding target. Using a SELEX procedure, we randomized and selected variants of a natural IHF site. We then analyzed these variants to determine how the 5' binding domain affects the structure, affinity, and function of an IHF-DNA complex in a native system. Despite finding individual sequences that varied over 100-fold in affinity for IHF, we found no apparent correlation between affinity and function. 相似文献
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Sanjay Chahar Vishal Gandhi Shiyan Yu Kinjal Desai Richard Cowper-Sal·lari Yona Kim Ansu O. Perekatt Namit Kumar Joshua K. Thackray Anthony Musolf Nikhil Kumar A. Hoffman Douglas Londono Berta N. Vazquez Lourdes Serrano Hyunjin Shin Mathieu Lupien Nan Gao Michael P. Verzi 《Molecular and cellular biology》2014,34(17):3291-3304
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trans meets cis in MADS science 总被引:10,自引:0,他引:10
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Searching for DNA-protein interactions by lambda phage display 总被引:5,自引:0,他引:5
Cicchini C Ansuini H Amicone L Alonzi T Nicosia A Cortese R Tripodi M Luzzago A 《Journal of molecular biology》2002,322(4):697-706