Prothymosin α interacts with the CREB-binding protein and potentiates transcription

Prothymosin α (ProTα) is a histone H1‐binding protein localized in sites of active transcription in the nucleus. We report here that ProTα physically interacts with the CREB‐binding protein (CBP), which is a versatile transcription co‐activator. Confocal laser scanning microscopy reveals that ProTα...

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Bibliographic Details
Published in:EMBO reports 2002-04, Vol.3 (4), p.361-366
Main Authors: Karetsou, Zoe, Kretsovali, Adroniki, Murphy, Carol, Tsolas, Orestes, Papamarcaki, Thomais
Format: Article
Language:English
Subjects:
Animals
Cattle
CREB-Binding Protein
Glutathione Transferase - metabolism
HeLa Cells
Humans
NF-kappa B - metabolism
Nuclear Proteins - metabolism
Precipitin Tests
Protein Precursors - metabolism
Rats
Scientific Report
Scientific Reports
Thymosin - analogs & derivatives
Thymosin - metabolism
Trans-Activators - metabolism
Transcription Factor AP-1 - metabolism
Transcription, Genetic - physiology
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Summary:Prothymosin α (ProTα) is a histone H1‐binding protein localized in sites of active transcription in the nucleus. We report here that ProTα physically interacts with the CREB‐binding protein (CBP), which is a versatile transcription co‐activator. Confocal laser scanning microscopy reveals that ProTα partially colocalizes with CBP in discrete subnuclear domains. Using transient transfections, we show that ProTα synergizes with CBP and stimulates AP1‐ and NF‐κB‐dependent transcription. Furthermore, overexpression of ProTα enhances the transactivation potential of CBP. These findings reveal a new function for ProTα in transcription activation, probably through CBP‐mediated recruitment to different promoters.
ISSN:1469-221X
1469-3178
DOI:10.1093/embo-reports/kvf071