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Vol. 12, No. 7, pp. 996-1009, April 1, 1998
1 Center for Cancer Research and Department of Biology,
Massachusetts Institute of Technology, Cambridge, Massachusetts 02139 USA;
2 Department of Cell Biology, University of Massachusetts
Medical School, Worcester, Massachusetts 01655 USA
The nuclear matrix antigen recognized by the monoclonal antibody
(mAb) B1C8 is a novel serine (S) and arginine (R)-rich protein associated with splicing complexes and is named here SRm160
(SR-related matrix protein of
160 kD). SRm160 contains multiple SR repeats, but unlike
proteins of the SR family of splicing factors, lacks an RNA recognition
motif. SRm160 and a related protein SRm300 (the 300-kD nuclear matrix
antigen recognized by mAb B4A11) form a complex that is required for
the splicing of specific pre-mRNAs. The SRm160/300
complex associates with splicing complexes and promotes splicing
through interactions with SR family proteins. Binding of
SRm160/300 to pre-mRNA is normally also dependent on U1
snRNP and is stabilized by U2 snRNP. Thus, SRm160/300
forms multiple interactions with components bound directly to important sites within pre-mRNA. The results suggest that a complex of the nuclear matrix proteins SRm160 and SRm300 functions as a coactivator of
pre-mRNA splicing.
[Key Words: Serine-arginine-rich splicing factor; small nuclear ribonucleoprotein particle; spliceosome; coactivator; nuclear matrix]
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