title: Molecular evolution of multisubunit RNA polymerases: structural analysis.
abstract: Comprehensive multiple sequence alignments of the multisubunit DNA-dependent RNA polymerase (RNAP) large subunits, including the bacterial beta and beta' subunits and their homologs from archaebacterial RNAPs, eukaryotic RNAPs I-III, nuclear-cytoplasmic large double-stranded DNA virus RNAPs, and plant plastid RNAPs, were created [Lane, W. J. and Darst, S. A. (2009). Molecular evolution of multisubunit RNA polymerases: sequence analysis. In press]. The alignments were used to delineate sequence regions shared among all classes of multisubunit RNAPs, defining common, fundamental RNAP features as well as identifying highly conserved positions. Here, we present a systematic, detailed structural analysis of these shared regions and highly conserved positions in terms of the RNAP structure, as well as the RNAP structure/function relationship, when known.
authors.affiliation: The Rockefeller University, Box 224, 1230 York Avenue, New York, NY 10065, USA.
authors.forename: William J
authors.initials: WJ
authors.lastname: Lane
authors.forename: Seth A
authors.initials: SA
authors.lastname: Darst
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D020134:Catalytic Domain; D017124:Conserved Sequence; D012321:DNA-Directed RNA Polymerases / Q000737:chemistry* / Q000235:genetics*; D019143:Evolution, Molecular; D005798:Genes, Bacterial; D005998:Glycine / Q000737:chemistry; D008958:Models, Molecular; D010802:Phylogeny; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D016963:Thermus thermophilus / Q000201:enzymology / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D021122:Protein Subunits; D012321:DNA-Directed RNA Polymerases; D005998:Glycine