Nucleic Acids Research, 2000, Vol. 28, No. 21 4299-4305
© 2000 Oxford University Press
Archaeal RNA polymerase subunits F and P are bona fide homologs of eukaryotic RPB4 and RPB12
Department of Biochemistry, Imperial College of Science, Technology and Medicine, Exhibition Road, London SW7 2AY, UK
The archaeal and eukaryotic evolutionary domains diverged from each other ~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.
* To whom correspondence should be addressed. Tel: +44 20 7594 5236; Fax: +44 20 7225 0960; Email: r.weinzierl@ic.ac.uk Present address: Jyrki Eloranta, Imperial Cancer Research Fund, Gene Transcription Laboratory, Hammersmith Hospital, Du Cane Road, London W12 0NN, UK
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