One Residue, Two Functions
The ETS family of transcription factors plays a variety of roles in development and differentiation. All members of the family have a highly conserved DNA-binding domain. In addition to binding to DNA, several members of the ETS family interact with other DNA-binding proteins, including members of the basic leucine zipper (bZIP) family. However, the molecular basis for this interaction has remained elusive.
Using Spi-1, one of the more diverse members of the ETS family, James A. Listman and colleagues demonstrated a novel mode of interaction for the ETS family transcription factors with the bZIP family of transcription factors. The authors convincingly showed that an arginine residue in Spi-1 that is essential for nuclear localization and corresponding DNA binding is also utilized for interaction with bZIP domains. These observations suggest new mechanisms of protein-protein and protein-DNA interactions for transcription factors. More...
Using Spi-1, one of the more diverse members of the ETS family, James A. Listman and colleagues demonstrated a novel mode of interaction for the ETS family transcription factors with the bZIP family of transcription factors. The authors convincingly showed that an arginine residue in Spi-1 that is essential for nuclear localization and corresponding DNA binding is also utilized for interaction with bZIP domains. These observations suggest new mechanisms of protein-protein and protein-DNA interactions for transcription factors. More...
posted by Selfmaderadio @ 1:37 e pasdites
