1PQV

RNA polymerase II-TFIIS complex

Summary for 1PQV

• Entry DOI: 10.2210/pdb1pqv/pdb
• Descriptor: DNA-directed RNA polymerase II largest subunit, DNA-directed RNA polymerases I, II, and III 8.3 kDa polypeptide, DNA-directed RNA polymerase II 13.6 kDa polypeptide, ... (15 entities in total)
• Functional Keywords: transcription, mrna cleavage, proofreading, backtracking, gene expression, multiprotein complex, protein soaking, transferase-transcription complex, transferase/transcription
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Nucleus: P04050 P38902 P07273 P08518 P16370 P20433 P20434 P34087 P20436 P27999; Nucleus, nucleolus: P22139 P40422; Cytoplasm: P20435
• Total number of polymer chains: 13
• Total formula weight: 548897.76

Authors

Kettenberger, H.,Armache, K.-J.,Cramer, P. (deposition date: 2003-06-19, release date: 2003-08-19, Last modification date: 2024-02-14)

Primary citation

Kettenberger, H.,Armache, K.-J.,Cramer, P.
Architecture of the RNA Polymerase II-TFIIS Complex and Implications for mRNA Cleavage
Cell(Cambridge,Mass.), 114:347-357, 2003

PubMed Abstract: The transcription elongation factor TFIIS induces mRNA cleavage by enhancing the intrinsic nuclease activity of RNA polymerase (Pol) II. We have diffused TFIIS into Pol II crystals and derived a model of the Pol II-TFIIS complex from X-ray diffraction data to 3.8 A resolution. TFIIS extends from the polymerase surface via a pore to the internal active site, spanning a distance of 100 A. Two essential and invariant acidic residues in a TFIIS loop complement the Pol II active site and could position a metal ion and a water molecule for hydrolytic RNA cleavage. TFIIS also induces extensive structural changes in Pol II that would realign nucleic acids in the active center. Our results support the idea that Pol II contains a single tunable active site for RNA polymerization and cleavage, in contrast to DNA polymerases with two separate active sites for DNA polymerization and cleavage.

PubMed: 12914699
DOI: 10.1016/S0092-8674(03)00598-1

Experimental method

X-RAY DIFFRACTION (3.8 Å)