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FF domains of CA150 bind transcription and splicing factors through multiple weak interactions.
- Source :
-
Molecular and cellular biology [Mol Cell Biol] 2004 Nov; Vol. 24 (21), pp. 9274-85. - Publication Year :
- 2004
-
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.
- Subjects :
- Amino Acid Motifs
Amino Acid Sequence
Amino Acid Substitution
Animals
Cell Line
Humans
Kinetics
Ligands
Mass Spectrometry
Mice
Molecular Sequence Data
Nuclear Proteins chemistry
Nuclear Proteins metabolism
Peptide Fragments chemistry
Peptide Fragments metabolism
Phosphoserine metabolism
Protein Binding
Protein Structure, Tertiary
RNA Polymerase II chemistry
RNA Polymerase II metabolism
Transcription Factors genetics
Transcriptional Elongation Factors
RNA Splicing genetics
Transcription Factors chemistry
Transcription Factors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0270-7306
- Volume :
- 24
- Issue :
- 21
- Database :
- MEDLINE
- Journal :
- Molecular and cellular biology
- Publication Type :
- Academic Journal
- Accession number :
- 15485897
- Full Text :
- https://doi.org/10.1128/MCB.24.21.9274-9285.2004