Nucleic Acids Research, Vol 25, Issue 11 2055-2061, Copyright © 1997 by Oxford University Press
JP Bourquin, I Stagljar, P Meier, P Moosmann, J Silke, T Baechi, O Georgiev and W Schaffner
The largest subunit of RNA polymerase II shows a striking difference in the
degree of phosphorylation, depending on its functional state: initiating
and elongating polymerases are unphosphorylated and highly phosphorylated
respectively. Phosphorylation mostly occurs at the C- terminal domain
(CTD), which consists of a repetitive heptapeptide structure. Using the
yeast two-hybrid system, we have selected for mammalian proteins that
interact with the phosphorylated CTD of mammalian RNA polymerase II. A
prominent isolate, designated SRcyp/CASP10, specifically interacts with the
CTD not only in vivo but also in vitro . It contains a serine/arginine-rich
(SR) domain, similar to that found in the SR protein family of pre-mRNA
splicing factors, which is required for interaction with the CTD. Most
remarkably, the N- terminal region of SRcyp includes a peptidyl-prolyl cis
- trans isomerase domain characteristic of immunophilins/cyclophilins
(Cyp), a protein family implicated in protein folding, assembly and
transport. SRcyp is a nuclear protein with a characteristic distribution in
large irregularly shaped nuclear speckles and co-localizes perfectly with
the SR domain-containing splicing factor SC35. Recent independent
investigations have provided complementary data, such as an association of
the phosphorylated form of RNA polymerase II with the nuclear speckles,
impaired splicing in a CTD deletion background and inhibition of in vitro
splicing by CTD peptides. Taken together, these data indicate that factors
directly or indirectly involved in splicing are associated with the
elongating RNA polymerases, from where they might translocate to the
nascent transcripts to ensure efficient splicing, concomitant with
transcription.
ARTICLES
A serine/arginine-rich nuclear matrix cyclophilin interacts with the C- terminal domain of RNA polymerase II
Institut fur Molekularbiologie, Abteilung II, Universitat Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.
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