The APT complex is involved in non-coding RNA transcription and is distinct from CPF

Research output: Contribution to journalArticle

Authors

  • Michael Lidschreiber
  • Ashley D. Easter
  • Sofia Battaglia
  • Juan B Rodríguez-Molina
  • Ana Casañal
  • Manuel Carminati
  • Carlo Baejen
  • Kerstin C. Maier
  • Patrick Cramer
  • Lori A Passmore

Colleges, School and Institutes

External organisations

  • Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry
  • Department of Biosciences and Nutrition, Center for Innovative Medicine and Science for Life Laboratory, Karolinska Institutet
  • MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
  • Karolinska Institutet, Department of Biosciences and Nutrition, Center for Innovative Medicine and Science for Life Laboratory, Novum, Hälsovägen 7, 141 83 Huddinge, Sweden.

Abstract

The 3'-ends of eukaryotic pre-mRNAs are processed in the nucleus by a large multiprotein complex, the cleavage and polyadenylation factor (CPF). CPF cleaves RNA, adds a poly(A) tail and signals transcription termination. CPF harbors four enzymatic activities essential for these processes, but how these are coordinated remains poorly understood. Several subunits of CPF, including two protein phosphatases, are also found in the related 'associated with Pta1' (APT) complex, but the relationship between CPF and APT is unclear. Here, we show that the APT complex is physically distinct from CPF. The 21 kDa Syc1 protein is associated only with APT, and not with CPF, and is therefore the defining subunit of APT. Using ChIP-seq, PAR-CLIP and RNA-seq, we show that Syc1/APT has distinct, but possibly overlapping, functions from those of CPF. Syc1/APT plays a more important role in sn/snoRNA production whereas CPF processes the 3'-ends of protein-coding pre-mRNAs. These results define distinct protein machineries for synthesis of mature eukaryotic protein-coding and non-coding RNAs.

Details

Original languageEnglish
Pages (from-to)11528–11538
JournalNucleic Acids Research
Volume46
Issue number21
Early online date21 Sep 2018
Publication statusPublished - 30 Nov 2018