Abstract
We show that the higher plant Arabidopsis thaliana has a serine-arginine-rich (SR) protein family whose members contain a phosphoepitope shared by the animal SR family of splicing factors. In addition, we report the cloning and characterization of a cDNA encoding a higher-plant SR protein from Arabidopsis, SR1, which has striking sequence and structural homology to the human splicing factor SF2/ASF. Similar to SF2/ASF, the plant SR1 protein promotes splice site switching in mammalian nuclear extracts. A novel feature of the Arabidopsis SR protein is a C-terminal domain containing a high concentration of proline, serine, and lysine residues (PSK domain), a composition reminiscent of histones. This domain includes a putative phosphorylation site for the mitotic kinase cyclin/p34cdc2.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Arabidopsis / metabolism*
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Arabidopsis Proteins*
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Arginine
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Base Sequence
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Cloning, Molecular
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DNA, Complementary
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Exons
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Humans
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Lysine
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Mammals
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Molecular Sequence Data
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Nuclear Proteins / biosynthesis*
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Plant Proteins / biosynthesis*
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Plant Proteins / chemistry
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Plant Proteins / genetics
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Proline
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RNA-Binding Proteins
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Sequence Homology, Amino Acid
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Serine
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Serine-Arginine Splicing Factors
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Spliceosomes / metabolism
Substances
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AT2G22300 protein, Arabidopsis
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Arabidopsis Proteins
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DNA, Complementary
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Nuclear Proteins
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Plant Proteins
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RNA-Binding Proteins
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Recombinant Proteins
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Serine-Arginine Splicing Factors
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Serine
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Arginine
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Proline
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Lysine