2C35

Subunits Rpb4 and Rpb7 of human RNA polymerase II

Summary for 2C35

• Entry DOI: 10.2210/pdb2c35/pdb
• Descriptor: DNA-DIRECTED RNA POLYMERASE II 16 KDA POLYPEPTIDE, DNA-DIRECTED RNA POLYMERASE II 19 KDA POLYPEPTIDE (3 entities in total)
• Functional Keywords: transcription, rna polymerase ii, polymerase, nucleotidyltransferase, transferase
• Biological source: HOMO SAPIENS (HUMAN); More
• Total number of polymer chains: 8
• Total formula weight: 146534.41

Authors

Meka, H.,Werner, F.,Cordell, S.C.,Onesti, S.,Brick, P. (deposition date: 2005-10-04, release date: 2005-11-18, Last modification date: 2023-12-13)

Primary citation

Meka, H.,Werner, F.,Cordell, S.C.,Onesti, S.,Brick, P.
Crystal Structure and RNA Binding of the Rpb4/Rpb7 Subunits of Human RNA Polymerase II.
Nucleic Acids Res., 33:6435-, 2005

PubMed Abstract: The Rpb4 and Rpb7 subunits of eukaryotic RNA polymerase II (RNAP(II)) form a heterodimer that protrudes from the 10-subunit core of the enzyme. We have obtained crystals of the human Rpb4/Rpb7 heterodimer and determined the structure to 2.7 A resolution. The presence of putative RNA-binding domains on the Rpb7 subunit and the position of the heterodimer close to the RNA exit groove in the 12 subunit yeast polymerase complex strongly suggests a role for the heterodimer in binding and stabilizing the nascent RNA transcript. We have complemented the structural analysis with biochemical studies directed at dissecting the RNA-binding properties of the human Rpb4/Rpb7 complex and that of the homologous E/F complex from Methanocaldococcus jannaschii. A number of conserved, solvent-exposed residues in both the human Rpb7 subunit and the archaeal E subunit have been modified by site-directed mutagenesis and the mutants tested for RNA binding by performing electrophoretic mobility shift assays. These studies have identified an elongated surface region on the corresponding face of both subunit E and Rpb7 that is involved in RNA binding. The area spans the nucleic acid binding face of the OB fold, including the B4-B5 loop, but also extends towards the N-terminal domain.

PubMed: 16282592
DOI: 10.1093/NAR/GKI945

Experimental method

X-RAY DIFFRACTION (2.7 Å)