2BZE

NMR Structure of human RTF1 PLUS3 domain.

Summary for 2BZE

• Entry DOI: 10.2210/pdb2bze/pdb
• NMR Information: BMRB: 7351
• Descriptor: KIAA0252 PROTEIN (1 entity in total)
• Functional Keywords: human rtf1 plus3 domain, transcription, elongation, paf1 complex, histone h3 methylation, h2b ubiquitination, cdc73, leo1, ctr9, plus3 domain, transcription regulation, structural proteomics in europe, spine, structural genomics
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 17567.15

Authors

Truffault, V.,Diercks, T.,Ab, E.,De Jong, R.N.,Daniels, M.A.,Kaptein, R.,Folkers, G.E.,Structural Proteomics in Europe (SPINE) (deposition date: 2005-08-16, release date: 2007-01-03, Last modification date: 2024-06-19)

Primary citation

De Jong, R.N.,Truffault, V.,Diercks, T.,Ab, E.,Daniels, M.A.,Kaptein, R.,Folkers, G.E.
Structure and DNA Binding of the Human Rtf1 Plus3 Domain.
Structure, 16:149-, 2008

PubMed Abstract: 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.

PubMed: 18184592
DOI: 10.1016/J.STR.2007.10.018

Experimental method

SOLUTION NMR