Bacterial RNA polymerase subunit omega and eukaryotic RNA polymerase subunit RPB6 are sequence, structural, and functional homologs and promote RNA polymerase assembly.
Bacterial DNA-dependent RNA polymerase (RNAP) has subunit composition beta'betaalpha(I)alpha(II)omega. The role of omega has been unclear. We show that omega is homologous in sequence and structure to RPB6, an essential subunit shared in eukaryotic RNAP I, II, and III. In Escherichia coli, overproduction of omega suppresses the assembly defect caused by substitution of residue 1362 of the largest subunit of RNAP, beta'. In yeast, overproduction of RPB6 suppresses the assembly defect caused by the equivalent substitution in the largest subunit of RNAP II, RPB1. High-resolution structural analysis of the omega-beta' interface in bacterial RNAP, and comparison with the RPB6-RPB1 interface in yeast RNAP II, confirms the structural relationship and suggests a "latching" mechanism for the role of omega and RPB6 in promoting RNAP assembly.
Pubmed ID: 11158566 RIS Download
Amino Acid Sequence | Archaea | Bacteria | Consensus Sequence | DNA-Directed RNA Polymerases | Databases as Topic | Models, Molecular | Molecular Sequence Data | Phosphoproteins | Protein Conformation | Protein Structure, Secondary | Protein Subunits | RNA Polymerase I | RNA Polymerase II | RNA Polymerase III | Recombinant Proteins | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Sequence Alignment | Sequence Homology, Amino Acid | Thermus