title: The Glc7 phosphatase subunit of the cleavage and polyadenylation factor is essential for transcription termination on snoRNA genes.
abstract: Glc7, the yeast protein phosphatase 1, is a component of the cleavage and polyadenylation factor (CPF). Here we show that downregulation of Glc7, or its dissociation from CPF in the absence of CPF subunits Ref2 or Swd2, results in similar snoRNA termination defects. Overexpressing a C-terminal fragment of Sen1, a superfamily I helicase required for snoRNA termination, suppresses the growth and termination defects associated with loss of Swd2 or Ref2, but not Glc7. Suppression by Sen1 requires nuclear localization and direct interaction with Glc7, which can dephosphorylate Sen1 in vitro. The suppressing fragment, and in a similar manner full-length Sen1, copurifies with the snoRNA termination factors Nrd1 and Nab3, suggesting loss of Glc7 from CPF can be compensated by recruiting Glc7 to Nrd1-Nab3 through Sen1. Swd2 is also a subunit of the Set1c histone H3K4 methyltransferase complex and is required for its stability and optimal methyltransferase activity.
authors.affiliation: Banting and Best Department of Medical Research, Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, ON M5S 3E1, Canada.
authors.forename: Eduard
authors.initials: E
authors.lastname: Nedea
authors.forename: Demet
authors.initials: D
authors.lastname: Nalbant
authors.forename: Daniel
authors.initials: D
authors.lastname: Xia
authors.forename: Nathaniel T
authors.initials: NT
authors.lastname: Theoharis
authors.forename: Bernhard
authors.initials: B
authors.lastname: Suter
authors.forename: Charles J
authors.initials: CJ
authors.lastname: Richardson
authors.forename: Kelly
authors.initials: K
authors.lastname: Tatchell
authors.forename: Thomas
authors.initials: T
authors.lastname: Kislinger
authors.forename: Jack F
authors.initials: JF
authors.lastname: Greenblatt
authors.forename: Peter L
authors.initials: PL
authors.lastname: Nagy
mesh_terms: D016923:Cell Death / Q000502:physiology; D004265:DNA Helicases; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D011495:Histone-Lysine N-Methyltransferase / Q000235:genetics / Q000378:metabolism; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism; D009687:Nuclear Proteins / Q000235:genetics / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000378:metabolism*; D054645:Protein Phosphatase 1; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism*; D020365:RNA Helicases; D012326:RNA Splicing; D020537:RNA, Small Nucleolar / Q000235:genetics* / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D012261:Ribonucleoproteins / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism; D014158:Transcription, Genetic; D039221:mRNA Cleavage and Polyadenylation Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D046912:Multiprotein Complexes; C090564:NAB3 protein, S cerevisiae; C491211:NRD1 protein, S cerevisiae; D009687:Nuclear Proteins; D021122:Protein Subunits; C092121:REF2 protein, S cerevisiae; D020537:RNA, Small Nucleolar; D016601:RNA-Binding Proteins; D012261:Ribonucleoproteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D039221:mRNA Cleavage and Polyadenylation Factors; D011495:Histone-Lysine N-Methyltransferase; C411250:SET1 protein, S cerevisiae; C484873:SWD2 protein, S cerevisiae; C092048:GLC7 protein, S cerevisiae; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1; C542347:SEN1 protein, S cerevisiae; D004265:DNA Helicases; D020365:RNA Helicases