Structure and DNA binding of the human Rtf1 Plus3 domain.
The yeast Paf1 complex consists of Paf1, Rtf1, Cdc73, Ctr9, and Leo1 and regulates histone H2B ubiquitination, histone H3 methylation, RNA polymerase II carboxy-terminal domain (CTD) Ser2 phosphorylation, and RNA 3' end processing. We provide structural insight into the Paf1 complex with the NMR structure of the conserved and functionally important Plus3 domain of human Rtf1. A predominantly beta-stranded subdomain displays structural similarity to Dicer/Argonaute PAZ domains and to Tudor domains. We further demonstrate that the highly basic Rtf1 Plus3 domain can interact in vitro with single-stranded DNA via residues on the rim of the beta sheet, reminiscent of siRNA binding by PAZ domains, but did not detect binding to double-stranded DNA or RNA. We discuss the potential role of Rtf1 Plus3 ssDNA binding during transcription elongation.
de Jong
Rob N
RN
Bijvoet Centre for Biomolecular Research, Utrecht University, Faculty of Chemistry, Department NMR Spectroscopy, Padualaan 8, Utrecht, The Netherlands.
Truffault
Vincent
V
Diercks
Tammo
T
Ab
Eiso
E
Daniels
Mark A
MA
Kaptein
Rob
R
Folkers
Gert E
GE
D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D004277:DNA, Single-Stranded / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009696:Nucleic Acids / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D016415:Sequence Alignment; D013491:Suppressor Factors, Immunologic / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics*; D014158:Transcription, Genetic; D006180:Proton-Translocating ATPases
D004277:DNA, Single-Stranded; D009696:Nucleic Acids; D013491:Suppressor Factors, Immunologic; D014157:Transcription Factors; C527330:RTF1 protein, human; C525845:ATP6V0A2 protein, human; D006180:Proton-Translocating ATPases