Abstract
The crystal structures of the Sulfolobus solfataricus (Sso) RNA polymerase and its subcomplex RpoD/RpoL have been determined at 3.4 and 1.76 Å resolution, respectively. In sharp contrast to the eukaryotic RNA polymerase II, the archael RNA polymerase has a deep DNA binding channel which may enable a transcription-competent open complex to form without the requirement of general transcription factors TFIIF and TFIIH. We also provide the first experimental evidence of an RNA polymerase possessing an iron-sulfur (Fe-S) cluster. Four cysteine residues in the Sso RpoD provide ligands for the Fe-S cluster, which is essential for proper RpoD folding to form a heterodimer with RpoL. This motif is conserved in other archaeal RNA polymerases and is also found in eukaryotic RNA polymerases I and III. The Fe-S cluster may provide a mechanism for detecting oxidative stress by the RNA polymerase. This study is supported by the Pew scholars program in the biomedical sciences.
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