Maf1 is a conserved inhibitor of RNA polymerase III (Pol III) that influences phenotypes ranging from metabolic efficiency to lifespan. Here, we present a 3.3-Å-resolution cryo-EM structure of yeast Maf1 bound to Pol III, establishing that Maf1 sequesters Pol III elements involved in transcription initiation and binds the mobile C34 winged helix 2 domain, sealing off the active site. The Maf1 binding site overlaps with that of TFIIIB in the preinitiation complex.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7104376 | PMC |
| http://dx.doi.org/10.1038/s41594-020-0383-y | DOI Listing |
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