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Literature DB >> 222478

E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA.

Abstract

The incubation of the E coli DNA binding protein HU with relaxed circular SV40 DNA in the presence of pure nicking-closing enzyme introduces up to 18 negative superhelical turns in the DNA molecules as measured by agarose gel electrophoresis. The maximal density of supercoiling is obtained at a HU-DNA mass ratio of 1. Reconstituted DNA-HU complexes prefixed with glutaraldehyde appear as condensed circular structures having an average of 14 "beads" per circular SV40 DNA molecule, with a "bead" diameter of 180 +/- 23 A. The circular SV40 DNA is condensed by a ratio of 2.0-2.5 relative to naked DNA. This is similar to the ratio (2.4) measured for chromatin formed by reassociation of relaxed SV40 DNA with the four core histones.

Entities: Chemical Gene Species

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Year: 1979 PMID： 222478 DOI： 10.1016/0092-8674(79)90152-1

Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582

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Cited

148 in total

1. The histone-like protein HU binds specifically to DNA recombination and repair intermediates.

Authors: D Kamashev; J Rouviere-Yaniv
Journal: EMBO J Date: 2000-12-01 Impact factor: 11.598

2. Massive parallel analysis of the binding specificity of histone-like protein HU to single- and double-stranded DNA with generic oligodeoxyribonucleotide microchips.

Authors: A S Krylov; O A Zasedateleva; D V Prokopenko; J Rouviere-Yaniv; A D Mirzabekov
Journal: Nucleic Acids Res Date: 2001-06-15 Impact factor: 16.971

3. The histone-like protein HU does not obstruct movement of T7 RNA polymerase in Escherichia coli cells but stimulates its activity.

Authors: Pilar Morales; Josette Rouviere-Yaniv; Marc Dreyfus
Journal: J Bacteriol Date: 2002-03 Impact factor: 3.490

4. Nonspecific DNA binding and bending by HUαβ: interfaces of the three binding modes characterized by salt-dependent thermodynamics.

Authors: Junseock Koh; Irina Shkel; Ruth M Saecker; M Thomas Record
Journal: J Mol Biol Date: 2011-04-12 Impact factor: 5.469

E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA.

1. The histone-like protein HU binds specifically to DNA recombination and repair intermediates.

2. Massive parallel analysis of the binding specificity of histone-like protein HU to single- and double-stranded DNA with generic oligodeoxyribonucleotide microchips.

3. The histone-like protein HU does not obstruct movement of T7 RNA polymerase in Escherichia coli cells but stimulates its activity.

4. Nonspecific DNA binding and bending by HUαβ: interfaces of the three binding modes characterized by salt-dependent thermodynamics.

5. MFP1 is a thylakoid-associated, nucleoid-binding protein with a coiled-coil structure.

Review 6. Chromosome partitioning in Escherichia coli.

7. Dual architectural roles of HU: formation of flexible hinges and rigid filaments.

8. Dividing a supercoiled DNA molecule into two independent topological domains.

9. Characterization of a histone-like protein extracted from yeast mitochondria.

10. Nicking-closing enzyme assembles nucleosome-like structures in vitro.