Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli.

作者：Josette Rouvière‐Yaniv, Francois Xavier Gros · 发表于：Proceedings of the National Academy of Sciences · 年份：1975 · DOI：10.1073/pnas.72.9.3428 · 被引用次数：336 · 研究领域：DNA and Nucleic Acid Chemistry、RNA and protein synthesis mechanisms、Click Chemistry and Applications

A low-molecular-weight (7000), heat-stable protein--HU--that stimulates transcription of bacteriophage lambda DNA by E. coli RNA polymerase was purified from E. coli extracts using affinity chromatography on DNA-cellulose. HU binds to native DNA, resulting in an apparent thickening of the DNA chains as revealed by electron microscopy. Contrary to DNA unwinding proteins, it causes no destabilization of the double helix. HU differs from previously described transcription factors (H1, D, etc.) and from the low-molecular-weight omega subunit of the RNA polymerase. By its amino-acid composition and characteristics, HU displays an interesting resemblance to some eukaryotic histones, such as H2B and H1.