The B-box dominates SAP-1–SRF interactions in the structure of the ternary complex
AUTOR(ES)
Hassler, Markus
FONTE
Oxford University Press
RESUMO
The serum response element (SRE) is found in several immediate-early gene promoters. This DNA sequence is necessary and sufficient for rapid transcriptional induction of the human c-fos proto-oncogene in response to stimuli external to the cell. Full activation of the SRE requires the cooperative binding of a ternary complex factor (TCF) and serum response factor (SRF) to their specific DNA sites. The X-ray structure of the human SAP-1–SRF–SRE DNA ternary complex was determined (Protein Data Bank code 1hbx). It shows SAP-1 TCF bound to SRF through interactions between the SAP-1 B-box and SRF MADS domain in addition to contacts between their respective DNA-binding motifs. The SAP-1 B-box is part of a flexible linker of which 21 amino acids become ordered upon ternary complex formation. Comparison with a similar region from the yeast MATα2–MCM1–DNA complex suggests a common binding motif through which MADS-box proteins may interact with additional factors such as Fli-1.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=150215Documentos Relacionados
- Saturation mutagenesis of the Drosophila tRNA(Arg) gene B-Box intragenic promoter element: requirements for transcription activation and stable complex formation.
- Comparative analysis of the ternary complex factors Elk-1, SAP-1a and SAP-2 (ERP/NET).
- Elk-1 can recruit SRF to form a ternary complex upon the serum response element.
- A protein domain conserved between yeast MCM1 and human SRF directs ternary complex formation.
- Selective response of ternary complex factor Sap1a to different mitogen-activated protein kinase subgroups.