title: Archaeal RNA polymerase subunits F and P are bona fide homologs of eukaryotic RPB4 and RPB12.
abstract: The archaeal and eukaryotic evolutionary domains diverged from each other approximately 2 billion years ago, but many of the core components of their transcriptional and translational machineries still display a readily recognizable degree of similarity in their primary structures. The F and P subunits present in archaeal RNA polymerases were only recently identified in a purified archaeal RNA polymerase preparation and, on the basis of localized sequence homologies, tentatively identified as archaeal versions of the eukaryotic RPB4 and RPB12 RNA polymerase subunits, respectively. We prepared recombinant versions of the F and P subunits from Methanococcus jannaschii and used them in in vitro and in vivo protein interaction assays to demonstrate that they interact with other archaeal subunits in a manner predicted from their eukaryotic counterparts. The overall structural conservation of the M. jannaschii F subunit, although not readily recognizable on the primary amino acid sequence level, is sufficiently high to allow the formation of an archaeal-human F-RPB7 hybrid complex.
authors.affiliation: Department of Biochemistry, Imperial College of Science, Technology and Medicine, Exhibition Road, London SW7 2AY, UK.
authors.forename: F
authors.initials: F
authors.lastname: Werner
authors.forename: J J
authors.initials: JJ
authors.lastname: Eloranta
authors.forename: R O
authors.initials: RO
authors.lastname: Weinzierl
mesh_terms: D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D019281:Dimerization; D005057:Eukaryotic Cells / Q000201:enzymology*; D006801:Humans; D046911:Macromolecular Substances; D017017:Methanococcus / Q000201:enzymology*; D008969:Molecular Sequence Data; D011485:Protein Binding; D021122:Protein Subunits; D012319:RNA Polymerase II / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D017385:Sequence Homology; D013379:Substrate Specificity; D013917:Thrombin / Q000378:metabolism; D020798:Two-Hybrid System Techniques
chemical_list: D019843:Archaeal Proteins; D046911:Macromolecular Substances; D021122:Protein Subunits; D011993:Recombinant Fusion Proteins; D029701:Saccharomyces cerevisiae Proteins; C491783:POLR2C protein, human; D012319:RNA Polymerase II; C112110:RPB3 protein, S cerevisiae; D013917:Thrombin