Crystal structure of RPB5, a universal eukaryotic RNA polymerase subunit and transcription factor interaction target.
Eukaryotic nuclei contain three different types of RNA polymerases (RNAPs), each consisting of 12-18 different subunits. The evolutionarily highly conserved RNAP subunit RPB5 is shared by all three enzymes and therefore represents a key structural/functional component of all eukaryotic RNAPs. Here we present the crystal structure of the RPB5 subunit from Saccharomyces cerevisiae. The bipartite structure includes a eukaryote-specific N-terminal domain and a C-terminal domain resembling the archaeal RNAP subunit H. RPB5 has been implicated in direct protein-protein contacts with transcription factor IIB, one of the components of the RNAP(II) basal transcriptional machinery, and gene-specific activator proteins, such as the hepatitis B virus transactivator protein X. The experimentally mapped regions of RPB5 involved in these interactions correspond to distinct and surface-exposed alpha-helical structures.
Todone
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Blackett Laboratory and Department of Biochemistry, Imperial College, Exhibition Road, London SW7 2AZ, United Kingdom.
Weinzierl
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Brick
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Onesti
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D000595:Amino Acid Sequence; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry*; D019281:Dimerization; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D012321:DNA-Directed RNA Polymerases