spacer gif spacer gif spacer gif spacer gif ARCHIVE ANNOUNCEMENT! spacer gif
 QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents    


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ovsenek, N.
Right arrow Articles by Heikkila, J. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ovsenek, N.
Right arrow Articles by Heikkila, J. J.

Development, Vol 110, Issue 2 427-433, Copyright © 1990 by Company of Biologists


JOURNAL ARTICLES

DNA sequence-specific binding activity of the heat-shock transcription factor is heat-inducible before the midblastula transition of early Xenopus development

N Ovsenek and JJ Heikkila
Department of Biology, University of Waterloo, Ontario, Canada.

We have examined the activity of the Xenopus heat-shock transcription factor (HSF) in extracts from stressed and unstressed embryos at various stages of development using DNA mobility shift analysis. A specific interaction between HSF and a synthetic oligonucleotide corresponding to the proximal heat-shock element (HSE) of the Xenopus HSP70B gene was greatly enhanced in heat-shocked embryos compared to controls. HSF binding was inducible at all developmental stages examined including pre-midblastula transition (MBT) stages which are incapable of expressing HSP genes. In time-course experiments with both cleavage and neurula stage embryos, the activation of HSF binding was rapid and transient. Removal of cleavage and neurula stage embryos from heat stress resulted in a rapid loss of binding activity. The molecular mass of HSF, as determined by comparative gel electrophoresis of photoaffinity-labeled factor was 88 x 10(3) in both heat-shocked cleavage and neurula stage embryos. These experiments suggest that maternally derived HSF is stored in pre-MBT embryos in a heat-activatable form and may function in the regulation of heat-shock genes immediately after the MBT.


This article has been cited by other articles:


Home page
Mol. Cell. Biol.Home page
S. Bharadwaj, A. Ali, and N. Ovsenek
Multiple Components of the HSP90 Chaperone Complex Function in Regulation of Heat Shock Factor 1 In Vivo
Mol. Cell. Biol., December 1, 1999; 19(12): 8033 - 8041.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
A. Ali, S. Bharadwaj, R. O'Carroll, and N. Ovsenek
HSP90 Interacts with and Regulates the Activity of Heat Shock Factor 1 in Xenopus Oocytes
Mol. Cell. Biol., September 1, 1998; 18(9): 4949 - 4960.
[Abstract] [Full Text]


Home page
J. Biol. Chem.Home page
P. A. Mercier, J. Foksa, N. Ovsenek, and J. T. Westwood
Xenopus Heat Shock Factor 1 Is a Nuclear Protein before Heat Stress
J. Biol. Chem., May 30, 1997; 272(22): 14147 - 14151.
[Abstract] [Full Text] [PDF]




© The Company of Biologists Ltd 1990