Robert P. Fisher

This study identifies tripartite phosphorylation of SPT5 by CDK9 as essential for regulating RNAPII transcription cycle phases, including pause release, elongation speed, and RNA processing.

This study reports the crystal structure of fully activated Cdk7/Cyclin H/Mat1 complex with dual T-loop phosphorylations, revealing their distinct roles in kinase activity and substrate recognition.

The paper identifies two Cdk9-phosphatase switches that regulate RNA polymerase II elongation and termination by modulating Spt5 phosphorylation at different stages of transcription.

The paper identifies a Cdk9-PP1 kinase-phosphatase switch that regulates the transition of RNA polymerase II from elongation to termination by modulating Spt5 phosphorylation.

This study investigates the role of Cdk9 in regulating RNA Polymerase II elongation rate using fission yeast and PRO-seq, finding that Cdk9 inhibition severely impairs early transcription but allows continued elongation.

The paper investigates the interaction between Cdk9, H2Bub1, and the Clr6-CII HDAC complex in regulating antisense and sense transcription in fission yeast.