PMID:8508774
| Citation |
Wang, Q and Calvo, JM (1993) Lrp, a major regulatory protein in Escherichia coli, bends DNA and can organize the assembly of a higher-order nucleoprotein structure. EMBO J. 12:2495-501 |
|---|---|
| Abstract |
Lrp (Leucine-responsive regulatory protein) is a global regulatory protein that controls the expression of many operons in Escherichia coli. One of those operons, ilvIH, contains six Lrp binding sites located within a several hundred base pair region upstream of the promoter region. Analysis of the binding of Lrp to a set of circularly permuted DNA fragments from this region indicates that Lrp induces DNA bending. The results of DNase I footprinting experiments suggest that Lrp binding to this region facilitates the formation of a higher-order nucleoprotein structure. To define more precisely the degree of bending associated with Lrp binding, one or two binding sites were separately cloned into a pBend vector and analyzed. Lrp induced a bend of approximately 52 degrees upon binding to a single binding site, and the angle of bending is increased to at least 135 degrees when Lrp binds to two adjacent sites. Lrp-induced DNA bending, and a natural sequence-directed bend that exists within ilvIH DNA, may be architectural elements that facilitate the assembly of a nucleoprotein complex. |
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| Keywords |
Bacterial Proteins/metabolism; Base Sequence; Binding Sites; DNA, Bacterial/chemistry; DNA, Bacterial/metabolism; DNA, Single-Stranded/chemistry; DNA, Single-Stranded/metabolism; DNA-Binding Proteins/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins; Leucine-Responsive Regulatory Protein; Molecular Sequence Data; Nucleic Acid Conformation; Nucleoproteins/chemistry; Nucleoproteins/metabolism; Operon; Promoter Regions, Genetic; Protein Binding; Regulatory Sequences, Nucleic Acid; Transcription Factors |
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