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Nucleic Acids Research, 2003, Vol. 31, No. 3 999-1005
© 2003 Oxford University Press

The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP

Paolo Licciardo, Stefano Amente, Luca Ruggiero, Maria Monti1, Piero Pucci1, Luigi Lania and Barbara Majello*

Department of Genetics, General and Molecular Biology and 1 Department of Organic Chemistry and Biochemistry, University of Naples ‘Federico II’, Via Mezzocannone 8, 80134 Naples, Italy

*To whom correspondence should be addressed. Tel: +39 081 2535003; Fax: +39 081 2535000; Email: majello{at}unina.it

RNA polymerase II transcription is associated with cyclic phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II. To date, FCP1 is the only specific CTD phosphatase, which is required for general transcription and cell viability. To identify FCP1-associated proteins, we constructed a human cell line expressing epitope-tagged FCP1. In addition to RAP74, a previously identified FCP1 interacting factor, we determined that FCP1-affinity purified extracts contain RNAPII that has either a hyper- or a hypo-phosphorylated CTD. In addition, by mass spectrometry of affinity purified FCP1-associated factors, we identified a novel FCP1-interacting protein, named MEP50, a recently described component of the methylosome complex that binds to the snRNP’s Sm proteins. We found that FCP1 specifically interacts with components of the spliceosomal U small nuclear ribonucleoproteins. These results suggest a putative role of FCP1 CTD-phosphatase in linking the transcription elongation with the splicing process.


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