Esther Harris
Howard Hughes Medical Institute
5 Papers
Esther Harris is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: DNA-binding domain & Binding site. The author has an hindex of 5, co-authored 5 publications. Previous affiliations of Esther Harris include Rockefeller University.
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Papers
Modular Organization of Pax/Homeodomain Proteins in Transcriptional Regulation
TL;DR: This work shows that, in a tissue culture system, a member of the Pax/HD family, Paired, is able to activate transcription after binding through either its PD or its HD, and shows that the Paired protein uses differently its C-terminal activation domain when transactivation is mediated through its PD and its HD.
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The homeodomain: a new face for the helix-turn-helix?
TL;DR: It is proposed that this intrinsic complexity of the HD, as well as its frequent association with other DNA binding domains, explains the functional specificity achieved by genes encoding highly related HDs.
A role for Gbx2 in repression of Otx2 and positioning the mid/hindbrain organizer.
Sandrine Millet,Kenneth Campbell,Kenneth Campbell,Douglas J. Epstein,Douglas J. Epstein,Kasia Losos,Esther Harris,Alexandra L. Joyner +7 more
TL;DR: It is proposed that formation of a normal MHB organizer depends on a sharp Otx2 caudal border and that Gbx2 is required to position and sharpen this border.
The paired box encodes a second DNA-binding domain in the paired homeo domain protein.
TL;DR: This work shows that the paired box of the prd gene encodes a DNA-binding activity, independent of the DNA- binding activity of the Paired (Prd) homeo domain and with a different sequence specificity, and destroys the ability of the Prd protein to bind to the paired domain-specific site.
A single amino acid can determine the DNA binding specificity of homeodomain proteins
TL;DR: It is shown that changing a single amino acid at the C-terminus of the recognition helix is both necessary and sufficient to confer the DNA binding specificity of either Ftz or Bcd on Prd, which contains two DNA binding activities.