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J. Biol. Chem., Vol. 280, Issue 41, 34435-34440, October 14, 2005

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Toward an Assembly Line for U7 snRNPs

INTERACTIONS OF U7-SPECIFIC Lsm PROTEINS WITH PRMT5 AND SMN COMPLEXES^*

Teldja N. Azzouz, Ramesh S. Pillai1, Christoph Däpp2, Ashwin Chari, Gunter Meister3, Christian Kambach¶, Utz Fischer, and Daniel Schümperli4

From the Institute of Cell Biology, University of Bern, Baltzerstrasse 4, 3012 Bern, Switzerland, Institute of Biochemistry, Biocenter of the University of Würzburg, Am Hubland, 97074 Würzburg, Germany, and ^¶Life Sciences, The Paul Scherrer Institute, 5232 Villigen PSI, Switzerland

The survival of motor neurons (SMN) complex mediates the assembly of small nuclear ribonucleoproteins (snRNPs) involved in splicing and histone RNA processing. A crucial step in this process is the binding of Sm proteins onto the SMN protein. For Sm B/B', D1, and D3, efficient binding to SMN depends on symmetrical dimethyl arginine (sDMA) modifications of their RG-rich tails. This methylation is achieved by another entity, the PRMT5 complex. Its pICln subunit binds Sm proteins whereas the PRMT5 subunit catalyzes the methylation reaction. Here, we provide evidence that Lsm10 and Lsm11, which replace the Sm proteins D1 and D2 in the histone RNA processing U7 snRNPs, associate with pICln in vitro and in vivo without receiving sDMA modifications. This implies that the PRMT5 complex is involved in an early stage of U7 snRNP assembly and hence may have a second snRNP assembly function unrelated to sDMA modification. We also show that the binding of Lsm10 and Lsm11 to SMN is independent of any methylation activity. Furthermore, we present evidence for two separate binding sites in SMN for Sm/Lsm proteins. One recognizes Sm domains and the second one, the sDMA-modified RG-tails, which are present only in a subset of these proteins.

Received for publication, May 9, 2005

^* This work was supported by the State of Bern, by Swiss National Science Foundation Grants 31-65225.01 and 3100A0-105547 (to D. S.), and by Grant SFB581 of the German Research Foundation (to U. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Present address: Friedrich Miescher Institute, Maulbeerstrasse 66, 4058, Basel, Switzerland.

² Present address: Institute of Anatomy, University of Bern, Baltzerstrasse 2, 3012 Bern, Switzerland.

³ Present address: Max-Planck-Institut für Biochemie, Am Klopferspitz 18, 82152 Martinsried, Germany.

⁴ To whom correspondence should be addressed. Tel.: 41-31-6314675; Fax: 41-31-6314616; E-mail: daniel.schuemperli{at}izb.unibe.ch.

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