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Journal ArticleDOI

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

02 Aug 1984-Nature (Nature Publishing Group)-Vol. 310, Iss: 5976, pp 376-381
TL;DR: The 3-Å structure of DNA-binding protein II, which exhibits histone-like properties in bacteria, has been determined and a mechanism by which the protein induces DNA supercoiling is proposed.
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.
Citations
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Journal ArticleDOI
06 Apr 1990-Cell
TL;DR: A cDNA clone that codes for a new tissue-specific DNA binding protein, PU.1, was isolated and was shown to be a transcriptional activator that is expressed in macrophages and B cells.

923 citations

Journal ArticleDOI
TL;DR: DNA bending induced by the H MG domain can facilitate the formation of higher-order nucleoprotein complexes, suggesting that HMG domain proteins may have an architectural role in assembling such complexes.

804 citations

Journal ArticleDOI
27 Dec 1996-Cell
TL;DR: The crystal structure of IHF complexed with 35 bp of DNA is reported, providing evidence for the importance of a narrow minor groove in IHF's binding sequence.

780 citations


Cites background from "3-Å resolution structure of a prote..."

  • ...To move the phosphate backbone out of the way of the neighboring same as that of HU (Tanaka et al., 1984; White et al., 1989): the bodies of the two proteins can be superim-complex, the bp 59 to the nick adopts a Hoogsteen configuration, and the one before that forms a reverse posed with a…...

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Journal ArticleDOI
25 Aug 1989-Cell
TL;DR: Human CTF/NF-I consists of a family of CCAAT box binding proteins that activate both transcription and DNA replication and analysis of cDNA mutants reveals that the N-terminal portion of CTF-1 is sufficient for site-specific DNA recognition, protein dimerization, and adenovirus replication.

701 citations

References
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Journal ArticleDOI
TL;DR: The molecular structures presented have the most probable values of bond-lengths, bond-angles and furanose ring conformations as defined by accurate X-ray crystallographic analyses of relevant monomers.

895 citations

Journal ArticleDOI
TL;DR: The gradual bimodal decrease in sedimentation rate seen after amino-acid starvation suggests that the faster sedimenting structures in exponentially growing cells represent the folded chromosomes at more advanced stages in their replication cycle.

587 citations

Journal ArticleDOI
30 Apr 1981-Nature
TL;DR: The three-dimensional structure of the 66-amino acid cro repressor protein of bacteriophage λ suggests how it binds to its operator DNA and suggests a pair of 2-fold-related α-helices of the represser seem to be a major determinant in recognition and binding.
Abstract: The three-dimensional structure of the 66-amino acid cro repressor protein of bacteriophage λ suggests how it binds to its operator DNA. We propose that a dimer of cro protein is bound to the B-form of DNA with the 2-fold axis of the dimer coincident with the 2-fold axis of DNA. A pair of 2-fold-related α-helices of the represser, lying within successive major grooves of the DNA, seem to be a major determinant in recognition and binding. In addition, the C-terminal residues of the protein, some of which are disordered in the absence of DNA, appear to contribute to the binding.

486 citations

Journal ArticleDOI
29 Jul 1982-Nature
TL;DR: Model-building studies of the repressor–operator complex suggest that α-helices, especially the N-terminal parts of these helices, may provide a useful surface for protein–DNA interactions.
Abstract: The structure of the operator-binding domain of the λ repressor has been determined at 3.2 A resolution. This domain contains an extended N-terminal arm and five α-helices. Model-building studies of the repressor–operator complex suggest that α-helices, especially the N-terminal parts of these helices, may provide a useful surface for protein–DNA interactions.

462 citations

Journal ArticleDOI
01 Jun 1979-Cell
TL;DR: 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.

431 citations