Temperature-dependent increase in the DNA-binding activity of a heat shock factor in an extract of tobacco cultured cells.
The DNA-binding activity of a tobacco heat shock factor (HSF) was induced by heat treatment (37-40 degrees C) of a cell-free extract that contained extra-nuclear fraction, but not in an extract of isolated nuclei. These observations suggest that an inactive form of HSF can directly recognize and transduce the heat shock signal and that such transduction requires components of the extranuclear fraction. Addition of ATP or of most other nucleoside triphosphates reduced the binding of the HSF to the heat shock element (HSE) in the same extract, and removal of ATP by dialysis from the extract restored the ability of the HSF to bind to DNA. The restored activity of the HSF could be eliminated again by a second addition of ATP. Our observations provide the first example of the involvement of ATP in the regulation of the reversible changes in HSF that control its ability to bind to HSEs in a cell-free extract.
Shimizu
S
S
School of Agricultural Sciences, Nagoya University, Japan.
Itoh
Y
Y
Yamazaki
K
K
D000255:Adenosine Triphosphate / Q000378:metabolism; D001483:Base Sequence; D002474:Cell-Free System; D002478:Cells, Cultured; D018744:DNA, Plant; D004268:DNA-Binding Proteins / Q000378:metabolism*; D017930:Genes, Reporter; D006360:Heat-Shock Proteins / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature; D008969:Molecular Sequence Data; D010947:Plants, Toxic; D011401:Promoter Regions, Genetic; D014026:Nicotiana / Q000166:cytology / Q000378:metabolism*
D018744:DNA, Plant; D004268:DNA-Binding Proteins; D006360:Heat-Shock Proteins; D000255:Adenosine Triphosphate