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THE PLANT CELL, Vol 8, Issue 12 2255-2264, Copyright © 1996 by American Society of Plant Biologists
Characterization of a Novel Arginine/Serine-Rich Splicing Factor in Arabidopsis
S. Lopato, E. Waigmann and A. Barta
Institute of Biochemistry, University of Vienna, Vienna Biocenter, Dr. Bohrgasse 9, A-1030 Vienna, Austria
Many splicing factors in vertebrate nuclei belong to a class of
evolutionarily conserved proteins containing arginine/serine (RS) or
serine/arginine (SR) domains. Previously, we demonstrated the existence of
SR splicing factors in plants. In this article, we report on a novel member
of this splicing factor family from Arabidopsis designated atRSp31. It has
one N-terminal RNA recognition motif and a C-terminal RS domain highly
enriched in arginines. The RNA recognition motif shows significant homology
to all animal SR proteins identified to date, but the intermediate region
does not show any homology to any other known protein. Subsequently, we
characterized two cDNAs from Arabidopsis that are highly homologous to
atRSp31 (designated atRSp35 and atRSp41). Their deduced amino acid
sequences indicate that these proteins constitute a new family of RS domain
splicing factors. Purified recombinant atRSp31 is able to restore splicing
in SR protein-deficient human S100 extracts. This indicates that atRSp31 is
a true plant splicing factor and plays a crucial role in splicing, similar
to that of other RS splicing factors. All of the three genes are
differentially expressed in a tissue-specific manner. The isolation of this
new plant splicing factor family enlarges the essential group of RS domain
splicing factors. Furthermore, because no animal equivalent to this protein
family has been identified to date, our results suggest that these proteins
play key roles in constitutive and alternative splicing in plants.
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