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Literature DB >> 6540370

3-A resolution structure of a protein with histone-like properties in prokaryotes.

I Tanaka, K Appelt, J Dijk, S W White, K S Wilson.

Abstract

The 3-A structure of DNA-binding protein II, which exhibits histone-like properties in bacteria, has been determined. The molecule is dimeric and appears to bind to the phosphate backbone of DNA through two symmetry-related arms. A mechanism by which the protein induces DNA supercoiling is proposed.

Entities: Chemical

Mesh：

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Year: 1984 PMID： 6540370 DOI： 10.1038/310376a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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Cited

90 in total

1. Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA.

Authors: A Tapias; G López; S Ayora
Journal: Nucleic Acids Res Date: 2000-01-15 Impact factor: 16.971

2. 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

3. Joint refinement as a tool for thorough comparison between NMR and X-ray data and structures of HU protein.

Authors: M L Raves; J F Doreleijer; H Vis; C E Vorgias; K S Wilson; R Kaptei
Journal: J Biomol NMR Date: 2001-11 Impact factor: 2.835

4. Recruitment of HU by piggyback: a special role of GalR in repressosome assembly.

Authors: S Kar; S Adhya
Journal: Genes Dev Date: 2001-09-01 Impact factor: 11.361

5. Histone-like proteins of the dinoflagellate Crypthecodinium cohnii have homologies to bacterial DNA-binding proteins.

Authors: J T Y Wong; D C New; J C W Wong; V K L Hung
Journal: Eukaryot Cell Date: 2003-06

6. 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

3-A resolution structure of a protein with histone-like properties in prokaryotes.

1. Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein which bridges DNA.

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

3. Joint refinement as a tool for thorough comparison between NMR and X-ray data and structures of HU protein.

4. Recruitment of HU by piggyback: a special role of GalR in repressosome assembly.

5. Histone-like proteins of the dinoflagellate Crypthecodinium cohnii have homologies to bacterial DNA-binding proteins.

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

7. Flexible DNA bending in HU-DNA cocrystal structures.

8. DNA binding and cleavage by the periplasmic nuclease Vvn: a novel structure with a known active site.

9. A mutation outside the two zinc fingers of ADR1 can suppress defects in either finger.

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