Differences in DNA-sequence recognition between the DNA-binding domain fragment and the full-length molecule of the heat-shock transcription factor of schistosome

Binding and inhibition studies reveal that the DNA-binding domain (DBD) fragment and the full-length molecule of the heat-shock transcription factor of schistosome (SmHSF) differ in DNA sequence recognition. SmHSF does not recognize the ideal HSE consensus sequence (nGAAnnTTCnnGAAn) but recognizes a...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2001-06, Vol.1519 (3), p.230-234
Main Authors: Lardans, Vinca, Ram, Daniela, Lantner, Frida, Ziv, Etty, Schechter, Israel
Format: Article
Language:English
Subjects:
Animals
Base Sequence
DNA binding domain
DNA sequence recognition
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Heat shock factor
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - genetics
Heat-Shock Proteins - metabolism
Molecular Sequence Data
Parasitic helminth
Schistosoma mansoni
Schistosoma mansoni - metabolism
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Summary:Binding and inhibition studies reveal that the DNA-binding domain (DBD) fragment and the full-length molecule of the heat-shock transcription factor of schistosome (SmHSF) differ in DNA sequence recognition. SmHSF does not recognize the ideal HSE consensus sequence (nGAAnnTTCnnGAAn) but recognizes a variant HSE that contains nGTAn instead of nGAAn in the third pentamer. The DBD reacts efficiently with the ideal HSE sequence and with lower affinity with the variant HSE sequence. These findings suggest that elements inside and outside the DBD contribute to the DNA-binding specificity of HSF.
ISSN:0167-4781
0006-3002
1879-2634
DOI:10.1016/S0167-4781(01)00220-2