TY - JOUR
T1 - The APT complex is involved in non-coding RNA transcription and is distinct from CPF
AU - Lidschreiber, Michael
AU - Easter, Ashley D.
AU - Battaglia, Sofia
AU - Rodríguez-Molina, Juan B.
AU - Casanal, Ana
AU - Carminati, Manuel
AU - Baejen, Carlo
AU - Grzechnik, Pawel
AU - Maier, Kerstin C.
AU - Cramer, Patrick
AU - Passmore, Lori A.
N1 - Funding Information:
Starting grant no. 261151 to L.A.P.]; European Union’s Horizon 2020 research and innovation programme [ERC Consolidator grant agreement no. 725685 to L.A.P.]; Medical Research Council (MRC) [MC U105192715 to L.A.P.]; Woolf Fisher scholarship [to A.D.E.]; Center for Innovative Medicine (CIMED) at Karolinska Institutet [to M.L.]; Science for Life Laboratory (SciLifeLab) [to M.L.]; Deutsche Forschungsgemeinschaft [SFB860, SPP1935 to P.C.]; European Research Council Advanced Investigator Grant TRANSREGULON [693023 to P.C.]; Volkswagen Foundation [to P.C.]; Sir Henry Dale Fellowship jointly funded by the Wellcome Trust and the Royal Society [200473/Z/16/Z to P.G.]. Funding for open access charge: European Research Council [ERC Consolidator grant agreement no. 725685 to L.A.P.]. Conflict of interest statement. None declared.
Publisher Copyright:
© The Author(s) 2018.
PY - 2018
Y1 - 2018
N2 - 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 proteincoding pre-mRNAs. These results define distinct protein machineries for synthesis of mature eukaryotic protein-coding and non-coding RNAs.
AB - 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 proteincoding pre-mRNAs. These results define distinct protein machineries for synthesis of mature eukaryotic protein-coding and non-coding RNAs.
UR - http://www.scopus.com/inward/record.url?scp=85058403283&partnerID=8YFLogxK
U2 - 10.1093/nar/gky845
DO - 10.1093/nar/gky845
M3 - Article
C2 - 30247719
AN - SCOPUS:85058403283
SN - 0305-1048
VL - 46
SP - 11528
EP - 11538
JO - Nucleic acids research
JF - Nucleic acids research
IS - 21
ER -