Distinct roles for the two cGATA-1 finger domains.

AUTOR(ES)

Yang, H Y

RESUMO

We have generated and analyzed by functional assays mutations of the chicken erythroid transcription factor GATA-1. The cGATA-1 protein contains two related finger domains highly conserved across species and characteristic of the family of GATA-binding factors. We find that mutations in the C-terminal finger or adjacent basic region abolish sequence-specific DNA binding, confirming that this region constitutes a novel DNA-binding domain sufficient to recognize the consensus WGATAR motif. At least three separate regions outside of this finger II domain contribute in a cooperative manner to the trans-activation potential of the protein. As expected from previous results analyzing the mouse homolog, we find that the N-terminal finger plays a role in DNA binding by affecting the stability of the DNA-protein complex. In addition, we find mutations of finger I subtly altered in DNA-binding function which greatly diminish trans-activation. Our results support the notion that the GATA-1 protein must be positioned precisely on the GATA cis element to enable the activation of target genes.

Documentos Relacionados

• Interaction of the erythroid transcription factor cGATA-1 with a critical auto-regulatory element.
• Self-association of the erythroid transcription factor GATA-1 mediated by its zinc finger domains.
• The two zinc finger-like domains of GATA-1 have different DNA binding specificities.
• Human HSP70 promoter contains at least two distinct regulatory domains.
• The core promoter of mouse rDNA consists of two functionally distinct domains.