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Molecular and Cellular Biology, May 2002, p. 3219-3229, Vol. 22, No. 10
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.10.3219-3229.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Human U4/U6.U5 and U4atac/U6atac.U5 Tri-snRNPs Exhibit Similar Protein Compositions

Claudia Schneider, Cindy L. Will, Olga V. Makarova, Evgeny M. Makarov, and Reinhard Lührmann*

Department of Cellular Biochemistry, Max Planck Institute of Biophysical Chemistry, D-37077 Göttingen, Germany

Received 9 November 2001/ Returned for modification 14 January 2002/ Accepted 14 February 2002

In the U12-dependent spliceosome, the U4atac/U6atac snRNP represents the functional analogue of the major U4/U6 snRNP. Little information is available presently regarding the protein composition of the former snRNP and its association with other snRNPs. In this report we show that human U4atac/U6atac di-snRNPs associate with U5 snRNPs to form a 25S U4atac/U6atac.U5 trimeric particle. Comparative analysis of minor and major tri-snRNPs by using immunoprecipitation experiments revealed that their protein compositions are very similar, if not identical. Not only U5-specific proteins but, surprisingly, all tested U4/U6- and major tri-snRNP-specific proteins were detected in the minor tri-snRNP complex. Significantly, the major tri-snRNP-specific proteins 65K and 110K, which are required for integration of the major tri-snRNP into the U2-dependent spliceosome, were among those proteins detected in the minor tri-snRNP, raising an interesting question as to how the specificity of addition of tri-snRNP to the corresponding spliceosome is maintained. Moreover, immunodepletion studies demonstrated that the U4/U6-specific 61K protein, which is involved in the formation of major tri-snRNPs, is essential for the association of the U4atac/U6atac di-snRNP with U5 to form the U4atac/U6atac.U5 tri-snRNP. Subsequent immunoprecipitation studies demonstrated that those proteins detected in the minor tri-snRNP complex are also incorporated into U12-dependent spliceosomes. This remarkable conservation of polypeptides between minor and major spliceosomes, coupled with the absence of significant sequence similarity between the functionally analogous snRNAs, supports an evolutionary model in which most major and minor spliceosomal proteins, but not snRNAs, are derived from a common ancestor.

* Corresponding author. Mailing address: Max Planck Institute of Biophysical Chemistry, Department of Cellular Biochemistry, Am Faßberg 11, D-37077 Göttingen, Germany. Phone: 49 551 201 1407. Fax: 49 551 201 1197. E-mail: reinhard.luehrmann{at}mpi-bpc.mpg.de.

Molecular and Cellular Biology, May 2002, p. 3219-3229, Vol. 22, No. 10
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.10.3219-3229.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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