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Molecular and Cellular Biology, June 1999, p. 4113-4120, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

pICln Inhibits snRNP Biogenesis by Binding Core Spliceosomal Proteins

William T. Pu, Grigory B. Krapivinsky, Luba Krapivinsky, and David E. Clapham*

Howard Hughes Medical Institute, Children's Hospital, Harvard Medical School, Boston, Massachusetts

Received 8 December 1998/Returned for modification 4 February 1999/Accepted 15 March 1999

The U1, U2, U4, U5, and U6 small nuclear ribonucleoproteins (snRNPs) form essential components of spliceosomes, the machinery that removes introns from pre-mRNAs in eukaryotic cells. A critical initial step in the complex process of snRNP biogenesis is the assembly of a group of common core proteins (Sm proteins) on spliceosomal snRNA. In this study we show by multiple independent methods that the protein pICln associates with Sm proteins in vivo and in vitro. The binding of pICln to Sm proteins interferes with Sm protein assembly on spliceosomal snRNAs and inhibits import of snRNAs into the nucleus. Furthermore, pICln prevents the interaction of Sm proteins with the survival of motor neurons (SMN) protein, an interaction that has been shown to be critical for snRNP biogenesis. These findings lead us to propose a model in which pICln participates in the regulation of snRNP biogenesis, at least in part by interfering with Sm protein interaction with SMN protein.

* Corresponding author. Mailing address: Howard Hughes Medical Institute, Children's Hospital, Harvard Medical School, 1309 Enders, 320 Longwood Ave., Boston, MA 02115. Phone: (617) 355-6163. Fax: (617) 355-3692. E-mail: clapham{at}rascal.med.harvard.edu.

Molecular and Cellular Biology, June 1999, p. 4113-4120, Vol. 19, No. 6
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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