RNA Helicase A Mediates Association of CBP with RNA Polymerase II

The coactivator CBP has been proposed to stimulate the expression of certain signal-dependent genes via its association with RNA polymerase II complexes. Here we show that complex formation between CBP and RNA polymerase II requires RNA helicase A (RHA), a nuclear DNA/RNA helicase that is related to...

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Bibliographic Details
Published in:Cell 1997-09, Vol.90 (6), p.1107-1112
Main Authors: Nakajima, Toshihiro, Uchida, Chiharu, Anderson, Stephen F., Lee, Chee-Gun, Hurwitz, Jerard, Parvin, Jeffrey D., Montminy, Marc
Format: Article
Language:English
Subjects:
Animals
Cells, Cultured
Cyclic AMP Response Element-Binding Protein - analysis
Cyclic AMP Response Element-Binding Protein - metabolism
DNA, Complementary - metabolism
Drosophila
Gene Expression Regulation, Enzymologic - physiology
Humans
Male
Phosphoserine
Precipitin Tests
Protein Binding - physiology
RNA Helicases
RNA Nucleotidyltransferases - metabolism
RNA Polymerase II - analysis
RNA Polymerase II - metabolism
Transcription, Genetic - physiology
Transcriptional Activation
Zinc Fingers - physiology
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Summary:The coactivator CBP has been proposed to stimulate the expression of certain signal-dependent genes via its association with RNA polymerase II complexes. Here we show that complex formation between CBP and RNA polymerase II requires RNA helicase A (RHA), a nuclear DNA/RNA helicase that is related to the Drosophila male dosage compensation factor mle. In transient transfection assays, RHA was found to cooperate with CBP in mediating target gene activation via the CAMP responsive factor CREB. As a mutation in RHA that compromised its helicase activity correspondingly reduced CREB-dependent transcription, we propose that RHA may induce local changes in chromatin structure that promote engagement of the transcriptional apparatus on signal responsive promoters.
ISSN:0092-8674
1097-4172
DOI:10.1016/S0092-8674(00)80376-1