The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain
Article Abstract:
A study determines the solution structure of the Octamer-1 POU-specific domain by applying multidimensional nuclear magnetic resonance spectroscopy. The structure has strong similarities with the bacteriophage lambda repressor DNA-binding domain. However, the POU-specific domain has an unusual helix-turn-helix (HTH) structure that differs from the canonical HTH motif in the length of the first alpha helix and the turn. Thus, the complete POU domain is comprised of two physically connected but separate domains that belong to an individual family of HTH-containing DNA-binding proteins.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
User Contributions:
Comment about this article or add new information about this topic:
Topological selectivity in Xer site-specific recombination
Article Abstract:
Gel electrophoresis was done to study the product topology of Xer-mediated site-specific recombination at plasmid sites. The results showed that the product of deletion at pSC101 psi is a right-handed antiparallel 4-noded catenane while that of ColE1 cer deletion has the same topology but with only one of the pair of strands exchanged. It was also found that the synapsis traps three negative supercoils between recombining sites and that strand exchange promotes further negative topological node in the deletion reaction.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
User Contributions:
Comment about this article or add new information about this topic:
Small peptides activate the latent sequence-specific DNA binding function of p53
Article Abstract:
Biochemical evidence shows that small peptides derived from the negative regulatory domain of p53 activate the DNA-binding function of latent p53. Microinjection of normal cells with an antibody specific to the C-terminus promote sequence-specific DNA-binding without increasing the protein level. A model showing a highly specific peptide activation system of p53 in terms of allosteric and steric mechanisms is presented.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Crystal structure of the interleukin-4/receptor alpha chain complex reveals a mosaic binding interface. Solution structure and ligand-binding site of the SH3 domain of the p85-alpha subunit of phosphatidylinositol 3-kinase
- Abstracts: Mechanism of corepressor-mediated specific DNA binding by the purine repressor. RNA recognition: a family matter?
- Abstracts: Pinning down positional information: dorsal-ventral polarity in the Drosophila embryo. Passover: a gene required for synaptic connectivity in the giant fiber system of Drosophila
- Abstracts: In vivo evidence that transcription and splicing are coordinated by a recruiting mechanism. Systematic identification and analysis of exonic splicing silencers
- Abstracts: Chemokine receptors and HIV-1: an attractive pair? Spatially restricted activation of the SAX receptor by SCW modulates DPP/TKV signaling in Drosophila dorsal-ventral patterning