3CLJ

Structure of the RNA polymerase II CTD-interacting domain of Nrd1

Summary for 3CLJ

• Entry DOI: 10.2210/pdb3clj/pdb
• Descriptor: Protein NRD1, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: ctd-interacting domain, nucleus, phosphoprotein, rna polymerase ii binding protein, rna binding protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Nucleus (Potential): P53617
• Total number of polymer chains: 1
• Total formula weight: 18189.55

Authors

Vasiljeva, L.,Kim, M.,Mutschler, H.,Buratowski, S.,Meinhart, A. (deposition date: 2008-03-19, release date: 2008-07-29, Last modification date: 2024-02-21)

Primary citation

Vasiljeva, L.,Kim, M.,Mutschler, H.,Buratowski, S.,Meinhart, A.
The Nrd1-Nab3-Sen1 termination complex interacts with the Ser5-phosphorylated RNA polymerase II C-terminal domain.
Nat.Struct.Mol.Biol., 15:795-804, 2008

PubMed Abstract: RNA polymerase II (Pol II) in Saccharomyces cerevisiae can terminate transcription via several pathways. To study how a mechanism is chosen, we analyzed recruitment of Nrd1, which cooperates with Nab3 and Sen1 to terminate small nucleolar RNAs and other short RNAs. Budding yeast contains three C-terminal domain (CTD) interaction domain (CID) proteins, which bind the CTD of the Pol II largest subunit. Rtt103 and Pcf11 act in mRNA termination, and both preferentially interact with CTD phosphorylated at Ser2. The crystal structure of the Nrd1 CID shows a fold similar to that of Pcf11, but Nrd1 preferentially binds to CTD phosphorylated at Ser5, the form found proximal to promoters. This indicates why Nrd1 cross-links near 5' ends of genes and why the Nrd1-Nab3-Sen1 termination pathway acts specifically at short Pol II-transcribed genes. Nrd1 recruitment to genes involves a combination of interactions with CTD and Nab3.

PubMed: 18660819
DOI: 10.1038/nsmb.1468

Experimental method

X-RAY DIFFRACTION (2.1 Å)