Mapping and mutagenesis of the amino-terminal transcriptional repression domain of the Drosophila Krüppel protein.

• DOI: 10.1128/mcb.14.6.4057
• Publication Date: 2015-10-06T00:40:01Z
• Authors: J D Licht; W Hanna-Rose; J C Reddy; M A English; M Ro; M Grossel; R Shaknovich; U Hansen
• Keywords: Krüppel; Alanine

We previously demonstrated that the Drosophila Krüppel protein is a transcriptional repressor with separable DNA-binding and repression activities. In this study, minimal amino (N)-terminal region of was defined by transferring regions to heterologous protein, lacI protein. Fusion predicted alpha-helical from acids 62 92 in N terminus sufficient transfer activity. This putative alpha-helix has several hydrophobic surfaces, as well glutamine-rich surface. Mutants containing multiple acid substitutions glutamine residues essential for activity entire N-terminal regions. Furthermore, one point mutant only single on surface altered lysine abolished ability repress, indicating importance at residue 86 repression. The also contained an adjacent activation localized between 117. Finally, accordance predictions primary sequence similarity, even-skipped which six times more potent than mammalian cells, characterized. segment included stretch 11 consecutive alanine proline-rich region.