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The RNA Binding Motif Protein 15B (RBM1 B/OTT3) Is a Functional Competitor of Serine-Arginine (SR) Proteins and Antagonizes the Positive Effect of the CDK11p110 -Cyclin L2α Complex on Splicing.

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Title: The RNA Binding Motif Protein 15B (RBM1 B/OTT3) Is a Functional Competitor of Serine-Arginine (SR) Proteins and Antagonizes the Positive Effect of the CDK11p110 -Cyclin L2α Complex on Splicing.
Authors: Loyer, Pascal1,2, Busson, Adeline1, Trembley, Janeen H.2, Hyle, Judith2, Grenet, Jose2, Wei Zhao3, Ribault, Catherine1, Montier, Tristan4, Kidd, Vincent J.2, Lahti, Jill M.2 Jill.Lahti@stjude.org
Source: Journal of Biological Chemistry. 1/7/2011, Vol. 286 Issue 1, p147-159. 13p.
Subjects: Protein binding, RNA splicing, Molecular genetics, Epstein-Barr virus, Messenger RNA, Serine proteinases, Arginine
Abstract: Here, we report the identification of the RNA binding motif protein RBM15B/OTT3 as a new CDK11p110 binding partner that alters the effects of CDK11 on splicing. RBM15B was initially identified as a binding partner of the Epstein-Barr virus mRNA export factor and, more recently, as a cofactor of the nuclear export receptor NXF1. In this study, we found that RBM15B co-elutes with CDK11p110, cyclin L2α, and serine-arginine (SR) proteins, including SF2/ASF, in a large nuclear complex of ~1-MDa molecular mass following size exclusion chromatography. Using co-immunoprecipitation experiments and in vitro pulldown assays, we mapped two distinct domains of RBM15B that are essential for its direct interaction with the N-terminal extension of CDK11p110, cyclin L2α, and SR proteins such as 9G8 and SF2/ASF. Finally, we established that RBM15B is a functional competitor of the SR proteins SF2/ASF and 9G8, inhibits formation of the functional spliceosomal E complex, and antagonizes the positive effect of the CDK11p110-cyclin L2α complex on splicing both in vitro and in vivo. [ABSTRACT FROM AUTHOR]
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Database: Engineering Source
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Abstract:Here, we report the identification of the RNA binding motif protein RBM15B/OTT3 as a new CDK11p110 binding partner that alters the effects of CDK11 on splicing. RBM15B was initially identified as a binding partner of the Epstein-Barr virus mRNA export factor and, more recently, as a cofactor of the nuclear export receptor NXF1. In this study, we found that RBM15B co-elutes with CDK11p110, cyclin L2α, and serine-arginine (SR) proteins, including SF2/ASF, in a large nuclear complex of ~1-MDa molecular mass following size exclusion chromatography. Using co-immunoprecipitation experiments and in vitro pulldown assays, we mapped two distinct domains of RBM15B that are essential for its direct interaction with the N-terminal extension of CDK11p110, cyclin L2α, and SR proteins such as 9G8 and SF2/ASF. Finally, we established that RBM15B is a functional competitor of the SR proteins SF2/ASF and 9G8, inhibits formation of the functional spliceosomal E complex, and antagonizes the positive effect of the CDK11p110-cyclin L2α complex on splicing both in vitro and in vivo. [ABSTRACT FROM AUTHOR]
ISSN:00219258
DOI:10.1074/jbc.M110.192518