Affiliation:
1. Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Abstract
The 2.5 angstrom resolution x-ray crystal structure of the
Escherichia coli
RNA polymerase (RNAP) α subunit amino-terminal domain (αNTD), which is necessary and sufficient to dimerize and assemble the other RNAP subunits into a transcriptionally active enzyme and contains all of the sequence elements conserved among eukaryotic α homologs, has been determined. The αNTD monomer comprises two distinct, flexibly linked domains, only one of which participates in the dimer interface. In the αNTD dimer, a pair of helices from one monomer interact with the cognate helices of the other to form an extensive hydrophobic core. All of the determinants for interactions with the other RNAP subunits lie on one face of the αNTD dimer. Sequence alignments, combined with secondary-structure predictions, support proposals that a heterodimer of the eukaryotic RNAP subunits related to
Saccharomyces cerevisiae
Rpb3 and Rpb11 plays the role of the αNTD dimer in prokaryotic RNAP.
Publisher
American Association for the Advancement of Science (AAAS)
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