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FINE-STRUCTURE ANALYSES OF THE DROSOPHILA AND SACCHAROMYCES HEAT-SHOCK FACTOR - HEAT-SHOCK ELEMENT INTERACTIONS
Author(s): FERNANDES M, XIAO H, LIS JT
Source: NUCLEIC ACIDS RESEARCH    Volume: 22    Issue: 2    Pages: 167-173    Published: JAN 25 1994  
Times Cited: 97     References: 40     
Abstract: Heat shock genes are activated by the binding of the heat shock transcription factor (HSF) to heat shock elements (HSEs), consisting of arrays of the 5-bp unit NGAAN arranged as inverted repeats. Here, we have investigated the interaction of the 5-bp unit with HSFs of Drosophila and Saccharomyces. Mutations within the conserved, central trinucleotide GAA reduce the relative binding affinity of both HSFs. In addition, the base at position 1 (N1) also influences binding, with a strong preference for an A at this position. Methylation interference initially indicated that HSF contacts A1 in the minor groove, but interacts with the immediately adjacent base G2 in the major groove. Further characterization of this apparently abrupt minor to major groove transition by substitution of A1 with an inosine, shows that HSF contacts A1 in the major groove. We offer an explanation for this apparent contradiction and propose that HSF recognizes the HSE primarily through contacts within the major groove of the DNA helix. Finally, based on these observations and a re-evaluation of the base frequencies and criteria for consensus sequence assignment, we propose that the sequence AGAAN more accurately represents the consensus HSE motif.
Document Type: Article
Language: English
Addresses:
1. CORNELL UNIV, BIOCHEM MOLEC & CELL BIOL SECT, ITHACA, NY 14853 USA
Publisher: OXFORD UNIV PRESS UNITED KINGDOM, WALTON ST JOURNALS DEPT, OXFORD, ENGLAND OX2 6DP
Subject Category: Biochemistry & Molecular Biology
IDS Number: MV140
ISSN: 0305-1048
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