| | |  | | | | Record from Web of Science® | | | | | | |
| SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF CD2-GAL4 FROM SACCHAROMYCES-CEREVISIAE |
|
|
| Author(s): BALEJA JD, MARMORSTEIN R, HARRISON SC, WAGNER G |
| Source: NATURE Volume: 356 Issue: 6368 Pages: 450-453 Published: APR 2 1992 |
| Times Cited: 113 References: 26 |
| Abstract: THE GAL4 protein activates transcription of the genes required for galactose utilization in Saccharomyces cerevisiae 1. The protein, consisting of 881 amino acids, is dimeric when bound to one of the approximately twofold symmetrical DNA sites present in the galactose upstream activating sequence (UAS(G)) 2-5. Here we use two-dimensional NMR spectroscopy to determine the structure of an amino-terminal fragment of GAL4 (residues 1-65). This fragment, a monomer in solution, binds as a dimer specifically to UAS(G)-containing DNA. Residues 9-40 form a well defined, compact globular cluster, whereas residues 1-8 and 41-66 show considerable conformational mobility in the absence of DNA. The compact domain contains a motif in which six cysteines, located on two symmetrically related helix/extended strand units connected by a long loop, coordinate two central zinc ions, forming a bimetal-thiolate cluster 6-11. The zincs were replaced by NMR-active Cd-113 in most of our work and structural parameters are therefore derived from the Cd2-protein. The structure obtained for the GAL4 DNA-binding domain represents a novel DNA-binding motif. Essentially the same conformation is observed for the compact domain in solution using NMR techniques as was seen for the central core of the N-terminal fragment bound to DNA using crystallographic techniques 12. Thus, the core of the DNA-binding domain changes little upon binding DNA. |
| Document Type: Article |
| Language: English |
Addresses:
1. HARVARD UNIV, SCH MED, DEPT BIOL CHEM & MOLEC PHARMACOL, BOSTON, MA 02115 USA
2. HARVARD UNIV, HOWARD HUGHES MED INST, CAMBRIDGE, MA 02138 USA
3. HARVARD UNIV, DEPT BIOCHEM & MOLEC BIOL, CAMBRIDGE, MA 02138 USA |
| Publisher: MACMILLAN MAGAZINES LTD, PORTERS SOUTH, 4 CRINAN ST, LONDON, ENGLAND N1 9XW |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: HL830 |
| ISSN: 0028-0836 |
|
| | | | | | | | | Record from Web of Science® | | | | | | | | | |