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Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing.

ABSTRACT: Biochemical purification of a pre-mRNA splicing activity from HeLa cells that stimulates distal alternative 3' splice sites in a concentration-dependent manner resulted in the identification of RNPS1, a novel general activator of pre-mRNA splicing. RNPS1 cDNAs, encoding a putative nucleic-acid-binding protein of unknown function, were previously identified in mouse and human. RNPS1 is conserved in metazoans and has an RNA-recognition motif preceded by an extensive serine-rich domain. Recombinant human RNPS1 expressed in baculovirus functionally synergizes with SR proteins and strongly activates splicing of both constitutively and alternatively spliced pre-mRNAs. We conclude that RNPS1 is not only a potential regulator of alternative splicing but may also play a more fundamental role as a general activator of pre-mRNA splicing.

SUBMITTER: Mayeda A

PROVIDER: S-EPMC1171530 | biostudies-other | 1999 Aug

REPOSITORIES: biostudies-other

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Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing.

Mayeda A A Badolato J J Kobayashi R R Zhang M Q MQ Gardiner E M EM Krainer A R AR

The EMBO journal 19990801 16

Biochemical purification of a pre-mRNA splicing activity from HeLa cells that stimulates distal alternative 3' splice sites in a concentration-dependent manner resulted in the identification of RNPS1, a novel general activator of pre-mRNA splicing. RNPS1 cDNAs, encoding a putative nucleic-acid-binding protein of unknown function, were previously identified in mouse and human. RNPS1 is conserved in metazoans and has an RNA-recognition motif preceded by an extensive serine-rich domain. Recombinant ...[more]

PMID: 10449421

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