Larry J. Friedman

The paper uses single-molecule fluorescence microscopy to show that TFIIH dissociates from RNA polymerase II before Spt4/5 binds, indicating Spt4/5 does not actively displace TFIIH.

The paper shows that bacterial RNA polymerase's C-terminal domains accelerate DNA binding through a physical mechanism involving flexible tethers.

The paper uses single-molecule microscopy to show Mediator recruitment to promoters is synergistic when multiple activators bind, revealing a non-cooperative mechanism.

This paper identifies an Orc6 tethering interaction that enables ORC to switch binding sites during replication origin licensing, showing its role in helicase loading and cell-cycle regulation.

This study uses single-molecule microscopy to analyze SAGA co-activator dynamics during transcription activation, revealing two distinct modes of interaction with DNA and activators.

This study investigates how changing protein-DNA interactions enable ORC to switch DNA binding sites during replication origin licensing, revealing a stepwise mechanism involving DNA unbending, sliding, and reduced ORC stability.

The paper investigates how ORC phosphorylation inhibits helicase loading by preventing Mcm2-7 ring closure in budding yeast.

The paper shows a single ORC molecule can load two oppositely-oriented Mcm2-7 helicases through a coordinated process involving Cdt1 release and ORC rearrangement.

The paper uses single-molecule microscopy to study RNA polymerase II pre-initiation complex assembly, revealing branched pathways and unexpected dynamics involving activators and transcription factors.