A hyperphosphorylated form of the large subunit of RNA polymerase II is associated with splicing complexes and the nuclear matrix. | Zendy

M. Mortillaro | Zendy; Benjamin J. Blencowe | Zendy; Xiumei Wei | Zendy; H. Nakayasu | Zendy; Lei Du | Zendy; Stephen L. Warren | Zendy; Phillip A. Sharp | Zendy; Ronald Berezney | Zendy

Open Access

A hyperphosphorylated form of the large subunit of RNA polymerase II is associated with splicing complexes and the nuclear matrix.

Author(s) -

M. Mortillaro,

Benjamin J. Blencowe,

Xiumei Wei,

H. Nakayasu,

Lei Du,

Stephen L. Warren,

Phillip A. Sharp,

Ronald Berezney

Publication year - 1996

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.93.16.8253

Subject(s) - rna splicing , rna polymerase ii , small nuclear ribonucleoprotein , ribonucleoprotein , exonic splicing enhancer , microbiology and biotechnology , biology , splicing factor , nuclear matrix , rna , genetics , gene expression , dna , promoter , gene , chromatin

A hyperphosphorylated form of the largest subunit of RNA polymerase II (pol IIo) is associated with the pre-mRNA splicing process. Pol IIo was detected in association with a subset of small nuclear ribonucleoprotein particle and Ser-Arg protein splicing factors and also with pre-mRNA splicing complexes assembled in vitro. A subpopulation of pol IIo was localized to nuclear "speckle" domains enriched in splicing factors, indicating that it may also be associated with RNA processing in vivo. Moreover, pol IIo was retained in a similar pattern following in situ extraction of cells and was quantitatively recovered in the nuclear matrix fraction. The results implicate nuclear matrix-associated hyperphosphorylated pol IIo as a possible link in the coordination of transcription and splicing processes.

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