ArticleMolecular and cellular biology2004
FF domains of CA150 bind transcription and splicing factors through multiple weak interactions.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 69 citations in OpenAlex.
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- Regulation of Functional Protein Aggregation by Multiple Factors: Implications for the Amyloidogenic Behavior of the CAP Superfamily Proteins.International journal of molecular sciences · 2020Review
- Human Tat-specific factor 1 binds the HIV-1 genome and selectively transports HIV-1 RNAs.Molecular biology reports · 2020Article
- The HIV-1 Tat Protein Enhances Splicing at the Major Splice Donor Site.Journal of virology · 2018Article
- A single cysteine post-translational oxidation suffices to compromise globular proteins kinetic stability and promote amyloid formation.Redox biology · 2018Article
- Transcriptional Elongation Regulator 1 Affects Transcription and Splicing of Genes Associated with Cellular Morphology and Cytoskeleton Dynamics and Is Required for Neurite Outgrowth in Neuroblastoma Cells and Primary Neuronal Cultures.Molecular neurobiology · 2017Article
- The in vivo dynamics of TCERG1, a factor that couples transcriptional elongation with splicing.RNA (New York, N.Y.) · 2016Article
- Article
- Transcription elongation regulator 1 (TCERG1) regulates competent RNA polymerase II-mediated elongation of HIV-1 transcription and facilitates efficient viral replication.Retrovirology · 2013Article
- Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response.Nature reviews. Molecular cell biology · 2013Review
- Specific interaction of the transcription elongation regulator TCERG1 with RNA polymerase II requires simultaneous phosphorylation at Ser2, Ser5, and Ser7 within the carboxyl-terminal domain repeat.The Journal of biological chemistry · 2013Article
- The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain.PloS one · 2013Article
- The FF4 and FF5 domains of transcription elongation regulator 1 (TCERG1) target proteins to the periphery of speckles.The Journal of biological chemistry · 2012Article
- TCERG1 regulates alternative splicing of the Bcl-x gene by modulating the rate of RNA polymerase II transcription.Molecular and cellular biology · 2012Article
- Genome-wide analysis of self-renewal in Drosophila neural stem cells by transgenic RNAi.Cell stem cell · 2011Article
- Identification of Tat-SF1 cellular targets by exon array analysis reveals dual roles in transcription and splicing.RNA (New York, N.Y.) · 2011Article
- RNA processing and export.Cold Spring Harbor perspectives in biology · 2010Review
- Differential effects of sumoylation on transcription and alternative splicing by transcription elongation regulator 1 (TCERG1).The Journal of biological chemistry · 2010Article
- The transcriptional transactivator Tat selectively regulates viral splicing.Nucleic acids research · 2010Article
- Crystal structure of the three tandem FF domains of the transcription elongation regulator CA150.Journal of molecular biology · 2009Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human transcription factor CA150 modulates human immunodeficiency virus type 1 gene transcription and contains numerous signaling elements, including six FF domains. Repeated FF domains are present in several transcription and splicing factors and can recognize phosphoserine motifs in the C-terminal domain (CTD) of RNA polymerase II (RNAPII). Using mass spectrometry, we identify a number of nuclear binding partners for the CA150 FF domains and demonstrate a direct interaction between CA150 and Tat-SF1, a protein involved in the coupling of splicing and transcription. CA150 FF domains recognize multiple sites within the Tat-SF1 protein conforming to the consensus motif (D/E)(2/5)-F/W/Y-(D/E)(2/5). Individual FF domains are capable of interacting with Tat-SF1 peptide ligands in an equivalent and noncooperative manner, with affinities ranging from 150 to 500 microM. Repeated FF domains therefore appear to bind their targets through multiple weak interactions with motifs comprised of negatively charged residues flanking aromatic amino acids. The RNAPII CTD represents a consensus FF domain-binding site, contingent on generation of the requisite negative charges by phosphorylation of serines 2 and 5. We propose that CA150, through the dual recognition of acidic motifs in proteins such as Tat-SF1 and the phosphorylated CTD, could mediate the recruitment of transcription and splicing factors to actively transcribing RNAPII.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.