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| YEAST HEAT-SHOCK TRANSCRIPTION FACTOR CONTAINS A FLEXIBLE LINKER BETWEEN THE DNA-BINDING AND TRIMERIZATION DOMAINS - IMPLICATIONS FOR DNA-BINDING BY TRIMERIC PROTEINS |
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| Author(s): FLICK KE, GONZALEZ L, HARRISON CJ, NELSON HCM |
| Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 269 Issue: 17 Pages: 12475-12481 Published: APR 29 1994 |
| Times Cited: 46 References: 35 |
| Abstract: All heat shock transcription factors (HSFs) share two regions of homology, identified as the DNA binding and trimerization regions. The DNA binding region consists of two parts, an 89-amino-acid minimal DNA-binding domain and an additional 21 amino acids which are not necessary for specific DNA binding of a monomeric DNA-binding domain. These 21 amino acids may act as a flexible linker between the DNA-binding and trimerization domains. Saccharomyces cerevisiae HSF has an additional 52 amino acids between the proposed flexible linker and the trimerization domain. Deletion of this unique region has no effect on the structural integrity or essential in vivo functions of HSF. To investigate the role of the 21-amino-acid proposed linker a series of internal deletions was created in fragments containing the DNA-binding and trimerization domains. The deletions have no effect on the structural integrity of the protein as assayed by circular dichroism spectroscopy. However, alterations of the linker do affect affinity of trimeric HSF binding to its target DNA In addition, deletion of part or all of the proposed linker from full-length yeast HSF, an essential protein, disrupts growth of yeast. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV CALIF BERKELEY, DEPT MOLEC & CELLULAR BIOL, DIV BIOCHEM & MOLEC BIOL, STANLEY DONNER ASU, BERKELEY, CA 94720 USA |
| Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: NH716 |
| ISSN: 0021-9258 |
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