| | |  | | | | Record from Web of Science® | | | | | | |
| THE IDENTIFICATION OF ELEMENTS DETERMINING THE DIFFERENT DNA-BINDING SPECIFICITIES OF THE MADS BOX PROTEINS P67SRF AND RSRFC4 |
|
|
| Author(s): SHARROCKS AD, VONHESLER F, SHAW PE |
| Source: NUCLEIC ACIDS RESEARCH Volume: 21 Issue: 2 Pages: 215-221 Published: JAN 25 1993 |
| Times Cited: 45 References: 26 |
| Abstract: The human transcription factors p67SRF and RSRFC4 recognise similar but distinct binding sites which are found in the promoters of both muscle-specific and 'immediate early' genes. Both proteins share a common basic DNA-binding domain, which is defined by the MADS box homology region. The DNA-binding specificity of a truncated form of p67SRF (core(SRF)) can be converted to that of RSRFC4. Removal of residues immediately N-terminal to the MADS box relaxes the specificity of core(SRF) for its cognate sequence (CC(A/T)6GG) as it improves binding to the RSRFC4 site (CTA(A/T)4TAG). Moreover, the introduction of a single, additional mutation, K154E, into the N-terminal truncated derivative completes the change in specificity to the RSRFC4 binding site. It also influences the salt dependence,of DNA binding and ternary complex formation With p62TCF. However, residues at this position do not appear to be involved in direct base-pair recognition. These results indicate that although the DNA binding specificity of p67SRF can be converted to that of RSRFC4, the two proteins may bind DNA in different ways. Furthermore, they suggest that binding site specificity can be determined by an indirect mechanism involving residues which are not directly involved in base recognition. |
| Document Type: Article |
| Language: English |
Addresses:
1. MAX PLANCK INST IMMUNOBIOL, SPEMANN LABS, W-3800 FREIBURG, GERMANY |
| Publisher: OXFORD UNIV PRESS UNITED KINGDOM, WALTON ST JOURNALS DEPT, OXFORD, ENGLAND OX2 6DP |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: KK200 |
| ISSN: 0305-1048 |
|
| | | | | | | | | Record from Web of Science® | | | | | | | | | |