title: Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain.
abstract: Phosphorylation of the C-terminal domain (CTD) of RNA polymerase II controls the co-transcriptional assembly of RNA processing and transcription factors. Recruitment relies on conserved CTD-interacting domains (CIDs) that recognize different CTD phosphoisoforms during the transcription cycle, but the molecular basis for their specificity remains unclear. We show that the CIDs of two transcription termination factors, Rtt103 and Pcf11, achieve high affinity and specificity both by specifically recognizing the phosphorylated CTD and by cooperatively binding to neighboring CTD repeats. Single-residue mutations at the protein-protein interface abolish cooperativity and affect recruitment at the 3' end processing site in vivo. We suggest that this cooperativity provides a signal-response mechanism to ensure that its action is confined only to proper polyadenylation sites where Ser2 phosphorylation density is highest.
authors.affiliation: Department of Biochemistry, University of Washington, Seattle, Washington, USA.
authors.forename: Bradley M
authors.initials: BM
authors.lastname: Lunde
authors.forename: Steve L
authors.initials: SL
authors.lastname: Reichow
authors.forename: Minkyu
authors.initials: M
authors.lastname: Kim
authors.forename: Hyunsuk
authors.initials: H
authors.lastname: Suh
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Leeper
authors.forename: Fan
authors.initials: F
authors.lastname: Yang
authors.forename: Hannes
authors.initials: H
authors.lastname: Mutschler
authors.forename: Stephen
authors.initials: S
authors.lastname: Buratowski
authors.forename: Anton
authors.initials: A
authors.lastname: Meinhart
authors.forename: Gabriele
authors.initials: G
authors.lastname: Varani
mesh_terms: D000595:Amino Acid Sequence; D017124:Conserved Sequence; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D010768:Phosphoserine / Q000737:chemistry; D017354:Point Mutation; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D012319:RNA Polymerase II / Q000737:chemistry / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D000068103:Serine-Arginine Splicing Factors; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism*; D014158:Transcription, Genetic; D039221:mRNA Cleavage and Polyadenylation Factors / Q000737:chemistry / Q000378:metabolism*
chemical_list: C491211:NRD1 protein, S cerevisiae; D009687:Nuclear Proteins; C512637:PCF11 protein, S cerevisiae; D010446:Peptide Fragments; D016601:RNA-Binding Proteins; C553428:Rtt103 protein, S cerevisiae; C531982:SCAF8 protein, human; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D039221:mRNA Cleavage and Polyadenylation Factors; D000068103:Serine-Arginine Splicing Factors; D010768:Phosphoserine; D012319:RNA Polymerase II
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