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J. Cell Biol.,
Volume 143, Number 2, October 19, 1998 297-307
* Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724; Expression of most RNA polymerase II transcripts requires the coordinated execution of transcription, splicing, and 3' processing. We have previously
shown that upon transcriptional activation of a gene in
vivo, pre-mRNA splicing factors are recruited from nuclear speckles, in which they are concentrated, to sites
of transcription (Misteli, T., J.F. Cáceres, and D.L.
Spector. 1997. Nature. 387:523-527). This recruitment
process appears to spatially coordinate transcription
and pre-mRNA splicing within the cell nucleus. Here
we have investigated the molecular basis for recruitment by analyzing the recruitment properties of mutant
splicing factors. We show that multiple protein domains
are required for efficient recruitment of SR proteins
from nuclear speckles to nascent RNA. The two types
of modular domains found in the splicing factor SF2/
ASF exert distinct functions in this process. In living
cells, the RS domain functions in the dissociation of the
protein from speckles, and phosphorylation of serine
residues in the RS domain is a prerequisite for this
event. The RNA binding domains play a role in the association of splicing factors with the target RNA. These
observations identify a novel in vivo role for the RS domain of SR proteins and suggest a model in which protein phosphorylation is instrumental for the recruitment of these proteins to active sites of transcription in
vivo.
MRC Human Genetics Unit, Western General
Hospital, Edinburgh, EH4 2XU, United Kingdom; and § Department of Immunology, University of Texas M.D. Anderson
Cancer Research Center, Houston, Texas 77030
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