Eukaryotic RNA polymerase subunit RPB8 is a new relative of the OB family
Stephan Krapp1, Geoff Kelly1, Joachim Reischl1, Robert O. J. Weinzierl1, 2
& Stephen Matthews1, 3
1Department of Biochemistry, Imperial College of Science, Technology and Medicine, Exhibition Road, South Kensington, London SW7 2AY, UK.
2email: rweinzierl@ic.ac.uk
3email: s.j.matthews@ic.ac.uk
RNA polymerase II sub unit RPB8 is an essential subunit that is highly conserved throughout eukaryotic evolution and is present hi all three types of nuclear RNA polymerases. We report the first high resolution structural insight into eukaryotic RNA polymerase architecture with the solution structure of RPB8 from Saccharomyces cerevisiae. It consists of an eight stranded, antiparallel -barrel, four short helical regions and a large, unstructured omega-loop. The strands are connected in classic Greek-key fashion. The overall topology is unusual and contains a striking C2 rotational symmetry. Furthermore, it is most likely a novel associate of the oligonucleotide/oligosaccharide (OB) binding protein class.
-barrel, four short helical regions and a large, unstructured omega-loop. The strands are connected in classic Greek-key fashion. The overall topology is unusual and contains a striking C2 rotational symmetry. Furthermore, it is most likely a novel associate of the oligonucleotide/oligosaccharide (OB) binding protein class.
