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Article

Rtf1 Is a Multifunctional Component of the Paf1 Complex That Regulates Gene Expression by Directing Cotranscriptional Histone Modification

, &
Pages 6103-6115 | Received 02 May 2007, Accepted 08 Jun 2007, Published online: 27 Mar 2023
 

Abstract

Numerous transcription accessory proteins cause alterations in chromatin structure that promote the progression of RNA polymerase II (Pol II) along open reading frames (ORFs). The Saccharomyces cerevisiae Paf1 complex colocalizes with actively transcribing Pol II and orchestrates modifications to the chromatin template during transcription elongation. To better understand the function of the Rtf1 subunit of the Paf1 complex, we created a series of sequential deletions along the length of the protein. Genetic and biochemical assays were performed on these mutants to identify residues required for the various activities of Rtf1. Our results establish that discrete nonoverlapping segments of Rtf1 are necessary for interaction with the ATP-dependent chromatin-remodeling protein Chd1, promoting covalent modification of histones H2B and H3, recruitment to active ORFs, and association with other Paf1 complex subunits. We observed transcription-related defects when regions of Rtf1 that mediate histone modification or association with active genes were deleted, but disruption of the physical association between Rtf1 and other Paf1 complex subunits caused only subtle mutant phenotypes. Together, our results indicate that Rtf1 influences transcription and chromatin structure through several independent functional domains and that Rtf1 may function independently of its association with other members of the Paf1 complex.

We are grateful to Patrick Costa for experimental contributions to Fig. and , Jakub Svoboda and Rajna Simic for technical assistance, Judith Jaehning for the antibody directed against Paf1, and Fred Winston, Grant Hartzog, Daniel Finley, Rick Young, and Kevin Struhl for the gifts of plasmids, PCR primer information, and strains. We also thank Joe Martens and members of the Arndt laboratory for valuable discussions and critical reading of the manuscript.

This work was supported by NIH grant GM52593 to K.M.A.

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