A CPF-like phosphatase module links transcription termination to chromatin silencing.

We then searched for phosphatases among the APRF1 interactors, finding a highly significant interaction with TOPP4 ( Figure 2A ), a protein with very high homology to Glc7 and PP1 ( Figure S7 ) and proven phosphatase activity in vivo , 42 and C-terminal domain phosphatase-like 3 (CPL3), homolog to yeast FCP1, whose role in activating FRI complex activity has been reported. 43 We have experimentally validated the interaction between APRF1 and TOPP4 in planta using transient coIP in Nicotiana benthamiana leaves of TOPP4 pro :TOPP4-3xFLAG and APRF1 pro :APRF1-mVENUS ( Figure 2C ).

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