Targeted Recruitment of Set1 Histone Methylase by Elongating Pol II Provides a Localized Mark and Memory of Recent Transcriptional Activity

• Published in: Molecular cell Vol. 11; no. 3; pp. 709 - 719
• Main Authors: Ng, Huck Hui, Robert, François, Young, Richard A., Struhl, Kevin
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.03.2003
• Subjects: Blotting, Western; DNA Methylation; DNA Polymerase II - metabolism; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - metabolism; Genome, Fungal; Histone-Lysine N-Methyltransferase; Histones - metabolism; Ligases - metabolism; Methylation; Models, Genetic; Nuclear Proteins - metabolism; Open Reading Frames; Phosphorylation; Precipitin Tests; Protein Structure, Tertiary; RNA, Messenger - metabolism; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism; Serine - metabolism; TATA-Box Binding Protein - metabolism; Transcription Factors - chemistry; Transcription Factors - metabolism; Transcription, Genetic; Ubiquitin-Conjugating Enzymes
• ISSN: 1097-2765; 1097-4164
• DOI: 10.1016/S1097-2765(03)00092-3

Set1, the yeast histone H3-lysine 4 (H3-K4) methylase, is recruited by the Pol II elongation machinery to a highly localized domain at the 5′ portion of active mRNA coding regions. Set1 association depends upon the TFIIH-associated kinase that phosphorylates the Pol II C-terminal domain (CTD) and mediates the transition between initiation and elongation, and Set1 interacts with the form of Pol II whose CTD is phosphorylated at serine 5 but not serine 2. The Rtf1 and Paf1 components of the Pol II-associated Paf1 complex are also important for Set1 recruitment. Although the level of dimethylated H3-K4 is fairly uniform throughout the genome, the pattern of trimethylated H3-K4 strongly correlates with Set1 occupancy. Hypermethylated H3-K4 within the mRNA coding region persists for considerable time after transcriptional inactivation and Set1 dissociation from the chromatin, indicating that H3-K4 hypermethylation provides a molecular memory of recent transcriptional activity.