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Papers In Press, published online ahead of print August 14, 2002
J. Biol. Chem, 10.1074/jbc.M201784200
Submitted on February 22, 2002
Revised on August 13, 2002
Accepted on August 14, 2002
Department of Molecular Biology/Biological Sciences, Vanderbilt University, Nashville, TN 37235
Corresponding Author: James.G.Patton{at}vanderbilt.edu
SRrp86 is a unique member of the SR protein superfamily of splicing factors containing one RNA Recognition Motif (RRM) and two serine-arginine (SR) rich domains separated by an unusual glutamic acid-lysine (EK) rich region. Previously, we showed that SRrp86 could regulate alternative splicing by both positively and negatively modulating the activity of other SR proteins as long as the entire region encompassing the RS-EK-RS domains was intact. To further investigate the function and domains of SRrp86, we generated a series of chimeric proteins by swapping the RRMs and RS domains between SRrp86 and two canonical members of the SR superfamily, ASF/SF2 and SRp75. While domain swaps between SRrp86 and ASF/SF2 showed that the RRMs primarily determined splicing activity, swaps between SRrp86 and SRp75 demonstrated that the RS domains could also determine activity. Since SRp75 also has two RS domains but lacks the EK domain, we further investigated the role of the EK domain and found that it acts to repress splicing and splice site selection, both in vitro and in vivo. Incubation of extracts with peptides encompassing the EK-rich region inactivated splicing and insertion of the EK region into SRp75 abolished its ability to activate splicing. Thus, the unique EK domain of SRrp86 plays a modulatory role controlling RS domain function.
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