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Identification of a plant serine-arginine-rich protein similar to the mammalian splicing factor SF2/ASF.

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.

SUBMITTER: Lazar G

PROVIDER: S-EPMC41207 | biostudies-other | 1995 Aug

REPOSITORIES: biostudies-other

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Identification of a plant serine-arginine-rich protein similar to the mammalian splicing factor SF2/ASF.

Lazar G G Schaal T T Maniatis T T Goodman H M HM

Proceedings of the National Academy of Sciences of the United States of America 19950801 17

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 ext ...[more]

PMID: 7644475

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Growth hormone deficiency and splicing fidelity: two serine/arginine-rich proteins, ASF/SF2 and SC35, act antagonistically.

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Serine/arginine-rich splicing factors belong to a class of intrinsically disordered proteins.

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