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Published online before print February 15, 2006, 10.1101/gad.1390306
GENES & DEVELOPMENT 20:531-536, 2006
©2006 by Cold Spring Harbor Laboratory Press; ISSN 0890-9369/ $5.00
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RESEARCH COMMUNICATION

Human telomerase and Cajal body ribonucleoproteins share a unique specificity of Sm protein association

Dragony Fu and Kathleen Collins1

Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 94720, USA

Cajal bodies are nuclear structures that host RNA modification and assembly reactions. Some RNAs transit Cajal bodies, while others must concentrate in Cajal bodies to function. Here we report that at least a subfraction of human telomerase RNA and individual resident Cajal body RNAs is associated with Sm proteins. Surprisingly, of seven Sm proteins assembled into a heteroheptameric ring, only a subset copurifies telomerase and Cajal body ribonucleoproteins. We show that a Cajal body RNA localization motif determines this specificity. These discoveries expand the cellular repertoire of Sm protein assemblies and their involvement in ribonucleoprotein localization and function.

[Keywords: telomerase ribonucleoprotein; Smith autoantigen; Cajal bodies]

Received November 4, 2005; revised version accepted December 28, 2005.

Supplemental material is available at http://www.genesdev.org.

Article published online ahead of print. Article and publication date are at http://www.genesdev.org/cgi/doi/10.1101/gad.1390306.

1 Corresponding author.
E-MAIL kcollins{at}berkeley.edu; FAX (510) 643-6334.


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