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p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor
- Source :
- Biochemical and Biophysical Research Communications. 306:660-665
- Publication Year :
- 2003
- Publisher :
- Elsevier BV, 2003.
-
Abstract
- The androgen receptor (AR) has two transactivation functions that have been mapped to the N- and C-terminal domains and designated as activation function-1 (AF-1) and AF-2, respectively. While the molecular basis for AF-2 function has been well studied, little is known about AF-1 coregulators. Therefore, we attempted to identify AF-1-interacting proteins from HEK293 cells by biochemical purification followed by mass fingerprinting by matrix-assisted laser desorption ionization–time-of-flight mass spectrometry (MALDI–TOF MS). Purified AF-1 region-interacting proteins were found to contain nuclear RNA-binding protein p54 nrb , polypyrimidine tract-binding protein-associated splicing factor (PSF), paraspeckle protein 1 (PSP1), and PSP2, which are assumed to be involved in pre-mRNA processing. p54 nrb interacted with AR via the A/B domain in a ligand-dependent manner. Reflecting the physical interaction between p54 nrb and the AR A/B domain, AR AF-1 function was potentiated by p54 nrb . Our results suggest that p54 nrb functions as a coactivator of AR that potentiates transcription, and presumably splicing as well.
- Subjects :
- Transcriptional Activation
Recombinant Fusion Proteins
Biophysics
Peptide Mapping
Biochemistry
Cell Line
Transactivation
Splicing factor
Nuclear Matrix-Associated Proteins
Genes, Reporter
Transcription (biology)
Coactivator
Humans
Molecular Biology
Chemistry
HEK 293 cells
Nuclear Proteins
RNA-Binding Proteins
Paraspeckle
Cell Biology
Molecular biology
Protein Structure, Tertiary
Cell biology
DNA-Binding Proteins
Androgen receptor
Receptors, Androgen
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
RNA splicing
Octamer Transcription Factors
Protein Binding
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 306
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....7b66a02e14cf1f042358f9e988a27552