The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP
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...
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Published in | Nucleic acids research Vol. 31; no. 3; pp. 999 - 1005 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
England
Oxford University Press
01.02.2003
Oxford Publishing Limited (England) |
Subjects | |
Online Access | Get full text |
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Summary: | 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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Bibliography: | Received October 4, 2002; Revised and Accepted December 7, 2002 ark:/67375/HXZ-CVZFCTKH-Q To whom correspondence should be addressed. Tel: +39 081 2535003; Fax: +39 081 2535000; Email: majello@unina.it local:gkg197 istex:FAF9C7F32A387ECDE38FC3C857CECBFA56D9D87E ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0305-1048 1362-4962 1362-4962 |
DOI: | 10.1093/nar/gkg197 |