24 research outputs found
The Relationship Between Online Video Game Involvement and Gaming-Related Friendships Among Emotionally Sensitive Individuals
No full text
The intra- and inter-observer reliability of the CT-scan based X index to quantify glenoid bone loss in chronic anterior shoulder instability and its impact on decision making
No full textSpring-to-summer changes and regional variability of benthic processes in the western Canadian Arctic
No full textTHAP proteins target specific DNA sites through bipartite recognition of adjacent major and minor grooves
No full textTHAP-family C(2)CH zinc-coordinating DNA-binding proteins function in diverse eukaryotic cellular processes, such as transposition, transcriptional repression, stem-cell pluripotency, angiogenesis and neurological function. To determine the molecular basis for sequence-specific DNA recognition by THAP proteins, we solved the crystal structure of the Drosophila melanogaster P element transposase THAP domain (DmTHAP) complexed with a natural 10-base pair site. In contrast to C(2)H(2) zinc fingers, DmTHAP docks a conserved β-sheet into the major groove and a basic C-terminal loop into the adjacent minor groove. We confirmed specific protein-DNA interactions by mutagenesis and DNA binding assays. Sequence analysis of natural and in-vitro-selected binding sites suggests several THAPs (DmTHAP, human THAP1 and THAP9) recognize a bipartite TxxGGGx(A/T) consensus motif; homology suggests THAP proteins bind DNA through a bipartite interaction. These findings reveal the conserved mechanisms by which THAP-family proteins engage specific chromosomal target elements
