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The human Prp8 protein is a component of both U2- and U12-dependent spliceosomes

Published online by Cambridge University Press:  01 July 1999

HONGBO R. LUO ,
GILLES A. MOREAU ,
NATASHA LEVIN  and
MELISSA J. MOORE
HONGBO R. LUO
Affiliation:
Howard Hughes Medical Institute, Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02454-9110, USA
GILLES A. MOREAU
Affiliation:
Howard Hughes Medical Institute, Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02454-9110, USA Current address: Department of Cell Biology, University of Geneva, Geneva 4, Switzerland.
NATASHA LEVIN
Affiliation:
Howard Hughes Medical Institute, Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02454-9110, USA
MELISSA J. MOORE
Affiliation:
Howard Hughes Medical Institute, Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02454-9110, USA
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Abstract

This study reports the cloning, sequencing, and development of antisera against the human U5 snRNP 220-kDa protein or hPrp8p. Prp8p is the most highly conserved large nuclear protein known to date, but it is not related to any other protein. Southern, Northern, and expressed sequence tag analyses indicate that hPrp8p is encoded by a single gene. Prp8p is a core component of U5 snRNP and the U4/U6.U5 tri-snRNP, and antibodies raised against it immunoprecipitate both the major, U2-dependent and minor, U12-dependent spliceosomes. These spliceosomes, which excise different classes of introns, contain distinct sets of snRNAs overlapping only with U5 snRNA. Other than the core Sm proteins, hPrp8p is the first splicing factor shown to be common to both spliceosomes.

Keywords

pre-mRNA splicingPrp8pspliceosomeU12-dependent spliceosome
Type
Research Article
Information
RNA , Volume 5 , Issue 7 , July 1999 , pp. 893 - 908
Copyright
© 1999 RNA Society

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