Histone Deacetylases and Phosphorylated Polymerase II C-Terminal Domain Recruit Spt6 for Cotranscriptional Histone Reassembly

Author:

Burugula Bala Bharathi1,Jeronimo Célia2,Pathak Rakesh1,Jones Jeffery W.1,Robert François23,Govind Chhabi K.1

Affiliation:

1. Department of Biological Sciences, Oakland University, Rochester, Michigan, USA

2. Institut de recherches cliniques de Montréal, Montréal, Québec, Canada

3. Département de Médecine, Faculté de Médecine, Université de Montréal, Montréal, Québec, Canada

Abstract

ABSTRACT Spt6 is a multifunctional histone chaperone involved in the maintenance of chromatin structure during elongation by RNA polymerase II (Pol II). Spt6 has a tandem SH2 (tSH2) domain within its C terminus that recognizes Pol II C-terminal domain (CTD) peptides phosphorylated on Ser2, Ser5, or Try1 in vitro . Deleting the tSH2 domain, however, only has a partial effect on Spt6 occupancy in vivo , suggesting that more complex mechanisms are involved in the Spt6 recruitment. Our results show that the Ser2 kinases Bur1 and Ctk1, but not the Ser5 kinase Kin28, cooperate in recruiting Spt6, genome-wide. Interestingly, the Ser2 kinases promote the association of Spt6 in early transcribed regions and not toward the 3′ ends of genes, where phosphorylated Ser2 reaches its maximum level. In addition, our results uncover an unexpected role for histone deacetylases (Rpd3 and Hos2) in promoting Spt6 interaction with elongating Pol II. Finally, our data suggest that phosphorylation of the Pol II CTD on Tyr1 promotes the association of Spt6 with the 3′ ends of transcribed genes, independently of Ser2 phosphorylation. Collectively, our results show that a complex network of interactions, involving the Spt6 tSH2 domain, CTD phosphorylation, and histone deacetylases, coordinate the recruitment of Spt6 to transcribed genes in vivo .

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

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