JBC Transcription and Nuclear Factor Monoclonals

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J Biol Chem, Vol. 273, Issue 46, 30122-30130, November 13, 1998

The Identification of Two Drosophila K Homology Domain Proteins
KEP1 AND SAM ARE MEMBERS OF THE Sam68 FAMILY OF GSG DOMAIN PROTEINS

Marco Di FruscioDagger , Taiping ChenDagger , Sheida Bonyadiparallel , Paul Laskoparallel , and Stéphane RichardDagger

From the Dagger  Terry Fox Molecular Oncology Group, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, and Departments of Oncology, Medicine and Microbiology and Immunology, McGill University, Montreal, Quebec H3T 1E2 and the parallel  Department of Biology, McGill University, Montreal, Quebec H3A 1B1, Canada

Sam68 is a member of a growing family of RNA-binding proteins that contains an extended K homology (KH) domain embedded in a larger domain called the GSG (GRP33, Sam68, GLD1) domain. To identify GSG domain family members, we searched data bases for expressed sequence tags encoding related portions of the Sam68 KH domain. Here we report the identification of two novel Drosophila KH domain proteins, which we termed KEP1 (KH encompassing protein) and SAM. SAM bears sequence identity with mammalian Sam68 and may be the Drosophila Sam68 homolog. We demonstrate that SAM, KEP1, and the recently identified Drosophila Who/How are RNA-binding proteins that are able to self-associate into homomultimers. The GSG domain of KEP1 and SAM was necessary to mediate the RNA binding and self-association. To elucidate the cellular roles of these proteins, SAM, KEP1, and Who/How were expressed in mammalian and Drosophila S2 cells. KEP1 and Who/How were nuclear and SAM was cytoplasmic. The expression of KEP1 and SAM, but not Who/How, activated apoptotic pathways in Drosophila S2 cells. The identification of KEP1 and SAM implies that a large GSG domain protein family exists and helps redefine the boundaries of the GSG domain. Taken together, our data suggest that KEP1 and SAM may play a role in the activation or regulation of apoptosis and further implicate the GSG domain in RNA binding and oligomerization.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 1998 by the American Society for Biochemistry and Molecular Biology.