Open AccessInteraction of the Neurospora crassa heat shock factor with the heat shock element during heat shock and different developmental stages
Author(s) -
Meyer Ulf,
Monnerjahn Christian,
Techel Dieter,
Rensing Ludger
Publication year - 2000
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2000.tb09071.x
Subject(s) - neurospora crassa , crassa , heat shock factor , shock (circulatory) , heat shock protein , cytoplasm , electrophoretic mobility shift assay , biology , heat shock , microbiology and biotechnology , biophysics , biochemistry , hsp70 , transcription factor , medicine , gene , mutant
The interaction of the heat shock factor (HSF) with the heat shock element (HSE) was determined by a non‐radioactive electrophoretic mobility shift assay, in order to analyze HSF regulation in Neurospora crassa . HSF binds to HSE under normal, non‐stress conditions and is thus constitutively trimerized. Upon heat shock, the HSF–HSE complex shows a retarded mobility. This was also observed in Saccharomyces cerevisiae , where this mobility shift was shown to be due to HSF phosphorylation [Sorger and Pelham (1988) Cell 54, 855–864]. In N. crassa , HSE‐dependent electrophoretic mobility shift is temperature‐ and time‐dependent. Under normal growth conditions, the HSF is located in the cytoplasm as well as in the nucleus. In germinating conidia the HSF shows a retarded mobility typical for heat shock even at normal growth temperatures. No HSF‐dependent mobility shift was detectable in aerial hyphae.