title: Interaction between the RNA-dependent ATPase and  poly(A) polymerase subunits of the TRAMP complex  is mediated by short peptides and important for  snoRNA processing.
abstract: The RNA exosome is one of the main 3′ to 5′ exoribonucleases in eukaryotic cells. Although it is responsible for degradation or processing of a wide variety of substrate RNAs, it is very specific and distinguishes between substrate and non-substrate RNAs as well as between substrates that need to be 3′ processed and those that need to be completely degraded. This specificity does not appear to be determined by the exosome itself but rather by about a dozen other proteins. Four of these exosome cofactors have enzymatic activity, namely, the nuclear RNA-dependent ATPase Mtr4, its cytoplasmic paralog Ski2 and the nuclear non-canonical poly(A) polymerases, Trf4 and Trf5. Mtr4 and either Trf4 or Trf5 assemble into a TRAMP complex. However, how these enzymes assemble into a TRAMP complex and the functional consequences of TRAMP complex assembly remain unknown. Here, we identify an important interaction site between Mtr4 and Trf5, and show that disrupting the Mtr4/Trf interaction disrupts specific TRAMP and exosome functions, including snoRNA processing.
authors.forename: Jillian S
authors.initials: JS
authors.lastname: Losh
authors.forename: Alejandra Klauer
authors.initials: AK
authors.lastname: King
authors.forename: Jeremy
authors.initials: J
authors.lastname: Bakelar
authors.forename: Lacy
authors.initials: L
authors.lastname: Taylor
authors.forename: John
authors.initials: J
authors.lastname: Loomis
authors.forename: Jason A
authors.initials: JA
authors.lastname: Rosenzweig
authors.forename: Sean J
authors.initials: SJ
authors.lastname: Johnson
authors.forename: Ambro
authors.initials: A
authors.lastname: van Hoof
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D010455:Peptides / Q000502:physiology*; D011062:Polynucleotide Adenylyltransferase / Q000378:metabolism*; D011485:Protein Binding; D012323:RNA Processing, Post-Transcriptional / Q000502:physiology*; D020537:RNA, Small Nucleolar / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D020798:Two-Hybrid System Techniques
chemical_list: D010455:Peptides; D020537:RNA, Small Nucleolar; D029701:Saccharomyces cerevisiae Proteins; D011062:Polynucleotide Adenylyltransferase; D000251:Adenosine Triphosphatases; C027900:RNA-dependent ATPase