1975
DOI: 10.1073/pnas.72.9.3428
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Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli.

Abstract: A low-molecular-weight (7000), heat-stable protein-HU-that stimulates transcription of bacteriophage X 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 (HI, D, etc.) and from the lowmolecular… Show more

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Cited by 313 publications
(152 citation statements)
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“…They hence belong to those DNA-binding proteins biochemically detected in thylakoids and nucleoid fractions (Briat et al 1984;Bülow et al 1987;Nemoto et al 1988;Yurina et al 1988;Baumgartner and Mullet 1991) that could have functionally replaced the bacterial histone-like HU (for histone-like protein from E. coli strain U93) proteins which are involved in formation of nucleosome-like structures in bacterial chromosomes (Rouviere-Yaniv and Gross 1975). Among these proteins are several low molecular weight proteins (10-20 kDa) detected by cross-reaction with antibodies directed toward the bacterial HU (Briat et al 1984).…”
Section: Proteins Replacing Hu and Histonesmentioning
confidence: 99%
“…They hence belong to those DNA-binding proteins biochemically detected in thylakoids and nucleoid fractions (Briat et al 1984;Bülow et al 1987;Nemoto et al 1988;Yurina et al 1988;Baumgartner and Mullet 1991) that could have functionally replaced the bacterial histone-like HU (for histone-like protein from E. coli strain U93) proteins which are involved in formation of nucleosome-like structures in bacterial chromosomes (Rouviere-Yaniv and Gross 1975). Among these proteins are several low molecular weight proteins (10-20 kDa) detected by cross-reaction with antibodies directed toward the bacterial HU (Briat et al 1984).…”
Section: Proteins Replacing Hu and Histonesmentioning
confidence: 99%
“…The Escherichia coli HU protein is a major component of the bacterial nucleoid (1)(2)(3). This small basic histone-like protein that can introduce negative supercoiling into a close circular DNA molecule in the presence of topoisomerase I is highly conserved and found in all bacterial species (4 -7).…”
mentioning
confidence: 99%
“…HU belongs to the family of architectural nuclear proteins that control DNA topology by introducing bends into doublestranded (ds) 1 DNA and stabilize higher-order nucleoprotein complexes. HU resembles eukaryotic proteins of the high mobility group (HMG) class in its DNA binding properties because it binds dsDNA with low affinity and no sequence specificity.…”
mentioning
confidence: 99%
“…Several basic histone-like proteins have been isolated from E. coli (24)(25)(26)(27). Proteins H (27) and HU (24) are among those whose amino acid compositions are known.…”
Section: Resultsmentioning
confidence: 99%