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Molecular and Cellular Biology, May 2000, p. 3049-3057, Vol. 20, No. 9
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Identification and Characterization of a Novel Serine-Arginine-Rich Splicing Regulatory Protein

Daron C. Barnard and James G. Patton*

Department of Molecular Biology, Vanderbilt University, Nashville, Tennessee 37235

Received 13 December 1999/Returned for modification 19 January 2000/Accepted 11 February 2000

We have identified an 86-kDa protein containing a single amino-terminal RNA recognition motif and two carboxy-terminal domains rich in serine-arginine (SR) dipeptides. Despite structural similarity to members of the SR protein family, p86 is clearly unique. It is not found in standard SR protein preparations, does not precipitate in the presence of high magnesium concentrations, is not recognized by antibodies specific for SR proteins, and cannot complement splicing-defective S100 extracts. However, we have found that p86 can inhibit the ability of purified SR proteins to activate splicing in S100 extracts and can even inhibit the in vitro and in vivo activation of specific splice sites by a subset of SR proteins, including ASF/SF2, SC35, and SRp55. In contrast, p86 activates splicing in the presence of SRp20. Thus, it appears that pairwise combination of p86 with specific SR proteins leads to altered splicing efficiency and differential splice site selection. In all cases, such regulation requires the presence of the two RS domains and a unique intervening EK-rich region, which appear to mediate direct protein-protein contact between these family members. Full-length p86, but not a mutant lacking the RS-EK-RS domains, was found to preferentially interact with itself, SRp20, ASF/SF2, SRp55, and, to a slightly lesser extent, SC35. Because of the primary sequence and unique properties of p86, we have named this protein SRrp86 for SR-related protein of 86 kDa.

* Corresponding author. Mailing address: Department of Molecular Biology, Box 1820 Station B, Vanderbilt University, Nashville, TN 37235. Phone: (615) 322-4738. Fax: (615) 343-6707. E-mail: James.G.Patton{at}vanderbilt.edu.

Molecular and Cellular Biology, May 2000, p. 3049-3057, Vol. 20, No. 9
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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