An Escherichia coli Protein That Preferentially Binds to Sharply Curved DNA
We attempted to find Escherichia coli proteins which preferentially bind to a curved DNA sequence even in the presence of an excess amount of a non-curved DNA sequence as a competitor, mainly by means of a DNA-binding gel retardation assay. Since the two sequences used had nearly the same nucleotide...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1990-09, Vol.108 (3), p.420-425 |
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| container_end_page | 425 |
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| container_issue | 3 |
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| container_title | Journal of biochemistry (Tokyo) |
| container_volume | 108 |
| creator | Yamada, Hisami Muramatsu, Shuji Mizuno, Takeshi |
| description | We attempted to find Escherichia coli proteins which preferentially bind to a curved DNA sequence even in the presence of an excess amount of a non-curved DNA sequence as a competitor, mainly by means of a DNA-binding gel retardation assay. Since the two sequences used had nearly the same nucleotide compositions, including consecutive dA5 stretches, we reasoned that this strategy would allow us to identify proteins which preferentially recognize an overall DNA curvature. We purified such a protein from E. coli. Its preferential binding to the curved DNA was found to be inhibited by distamycin, which removes the curvature from appropriate DNA sequences. The purified protein was identified as the E. coli nucleoid protein, H-NS. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a123216 |
| format | Article |
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Since the two sequences used had nearly the same nucleotide compositions, including consecutive dA5 stretches, we reasoned that this strategy would allow us to identify proteins which preferentially recognize an overall DNA curvature. We purified such a protein from E. coli. Its preferential binding to the curved DNA was found to be inhibited by distamycin, which removes the curvature from appropriate DNA sequences. 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Since the two sequences used had nearly the same nucleotide compositions, including consecutive dA5 stretches, we reasoned that this strategy would allow us to identify proteins which preferentially recognize an overall DNA curvature. We purified such a protein from E. coli. Its preferential binding to the curved DNA was found to be inhibited by distamycin, which removes the curvature from appropriate DNA sequences. 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| fulltext | fulltext |
| identifier | ISSN: 0021-924X |
| ispartof | Journal of biochemistry (Tokyo), 1990-09, Vol.108 (3), p.420-425 |
| issn | 0021-924X 1756-2651 |
| language | eng |
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| source | MEDLINE; Oxford University Press Journals Digital Archive Legacy; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Bacterial Proteins - metabolism Base Sequence Binding and carrier proteins Binding, Competitive Biological and medical sciences Distamycins - pharmacology DNA - metabolism DNA-Binding Proteins - metabolism Escherichia coli - drug effects Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Molecular Sequence Data Molecular Weight Proteins |
| title | An Escherichia coli Protein That Preferentially Binds to Sharply Curved DNA |
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