Abstract:
:The minimal DNA sequence required for the formation of a stable complex with Drosophila heat shock factor (HSF) in vitro is an inverted repeat of a 5 bp recognition unit, -GAA-. Surprisingly, both permutations of this 5 bp unit, head-to-head and tail-to-tail, bind to HSF with similar affinity and with striking 2-fold symmetry. HSF also binds to longer arrays of inverted 5 bp units, and the size of the HSF footprint increases with the addition of each 5 bp unit to these arrays. However, the electrophoretic mobility of the HSF-DNA complexes decreases most distinctly with the addition of every three 5 bp units. Cross-linking of purified HSF in the absence of DNA generates complexes with the sizes expected of HSF trimers. We propose that trimers of HSF bind to DNA and that the number of HSF subunits in direct contact with DNA is determined by the number of correctly positioned 5 bp recognition units.
journal_name
Celljournal_title
Cellauthors
Perisic O,Xiao H,Lis JTdoi
10.1016/0092-8674(89)90603-xsubject
Has Abstractpub_date
1989-12-01 00:00:00pages
797-806issue
5eissn
0092-8674issn
1097-4172pii
0092-8674(89)90603-Xjournal_volume
59pub_type
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