PMID:8459763
| Citation |
Pontiggia, A, Negri, A, Beltrame, M and Bianchi, ME (1993) Protein HU binds specifically to kinked DNA. Mol. Microbiol. 7:343-50 |
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| Abstract |
We have purified the main four-way junction DNA-binding protein of Escherichia coli, and have found it to be the well-known HU protein. HU protein recognizes with high-affinity one of the angles present in the junction, a molecule with the shape of an X. Other DNA structures characterized by sharp bends or kinks, like bulged duplex DNAs containing unpaired bases, are also bound. HU protein appears to inhibit cruciform extrusion from supercoiled inverted repeat (palindromic) DNA, either by constraining supercoiling or by trapping a metastable interconversion intermediate. All these properties are analogous to the properties of the mammalian chromatin protein HMG1. We suggest that HU is a prokaryotic HMG1-like protein rather than a histone-like protein. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Base Sequence; Binding, Competitive; DNA, Bacterial/metabolism; DNA, Superhelical/metabolism; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/isolation & purification; DNA-Binding Proteins/metabolism; Endodeoxyribonucleases/metabolism; Escherichia coli/chemistry; High Mobility Group Proteins/chemistry; High Mobility Group Proteins/metabolism; Molecular Sequence Data; Nucleic Acid Conformation; Plasmids/metabolism; Repetitive Sequences, Nucleic Acid |
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