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Originally published In Press as doi:10.1074/jbc.M101360200 on March 13, 2001

J. Biol. Chem., Vol. 276, Issue 23, 20711-20718, June 8, 2001
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The Heterogeneous Nuclear Ribonucleoproteins I and K Interact with a Subset of the Ro Ribonucleoprotein-associated Y RNAs in Vitro and in Vivo*

Gustáv FabiniDagger §, Reinout Raijmakers||, Silvia HayerDagger §, Michael A. Fouraux||, Ger J. M. Pruijn||, and Günter SteinerDagger §**

From the Dagger  Institute of Medical Biochemistry, University of Vienna, the Vienna Biocenter, Dr. Bohr-Gasse 9, A-1030 Vienna, Austria, the § Division of Rheumatology, University Hospital of Vienna, Waehringer Guertel 18, A-1090 Vienna, Austria, and the || Department of Biochemistry, Nijmegen Center for Molecular Life Sciences, University of Nijmegen, NL-6500 HB Nijmegen, The Netherlands

The hY RNAs are a group of four small cytoplasmic RNAs of unknown function that are stably associated with at least two proteins, Ro60 and La, to form Ro ribonucleoprotein complexes. Here we show that the heterogeneous nuclear ribonucleoproteins (hnRNP) I and K are able to associate with a subset of hY RNAs in vitro and demonstrate these interactions to occur also in vivo in a yeast three-hybrid system. Experiments performed in vitro and in vivo with deletion mutants of hY1 RNA revealed its pyrimidine-rich central loop to be involved in interactions with both hnRNP I and K and clearly showed their binding sites to be different from the Ro60 binding site. Both hY1 and hY3 RNAs coprecipitated with hnRNP I in immunoprecipitation experiments performed with HeLa S100 extracts and cell extracts from COS-1 cells transiently transfected with VSV-G-tagged hnRNP-I, respectively. Furthermore, both anti-Ro60 and anti-La antibodies coprecipitated hnRNP I, whereas coprecipitation of hnRNP K was not observed. Taken together, these data strongly suggest that hnRNP I is a stable component of a subpopulation of Ro RNPs, whereas hnRNP K may be transiently bound or interact only with (rare) Y RNAs that are devoid of Ro60 and La. Given that functions related to translation regulation have been assigned to both proteins and also to La, our findings may provide novel clues toward understanding the role of Y RNAs and their respective RNP complexes.

* This work was supported by a grant from the Austrian Science Fund (project part no. 5 of the Special Research Project "Modulators of RNA Fate and Function") and in part by the Netherlands Foundation for Chemical Research with financial aid from the Netherlands Organization for Scientific Research.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Inst. of Chemistry, Div. of Glycobiology, Agricultural University, Muthgasse 18, A-1190 Vienna, Austria.

** To whom correspondence should be addressed: Div. of Rheumatology, Dept. of Internal Medicine III, University Hospital of Vienna, Waehringer Guertel 18-20, A-1090 Vienna, Austria. Tel.: 431-40400-2121; Fax: 431-40400-4306; E-mail: Guenter.Steiner@akh-wien.ac.at.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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