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J. Biol. Chem., Vol. 275, Issue 32, 24284-24293, August 11, 2000
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From the In animals, replication-dependent
histone genes are expressed in dividing somatic cells during S phase to
maintain chromatin condensation. Histone mRNA 3'-end formation is
an essential regulatory step producing an mRNA with a hairpin
structure at the 3'-end. This requires the interaction of the U7 small
nuclear ribonucleoprotein particle (snRNP) with a purine-rich spacer
element and of the hairpin-binding protein with the hairpin element,
respectively, in the 3'-untranslated region of histone RNA. Here, we
demonstrate that bona fide histone RNA 3' processing takes
place in Xenopus egg extracts in a reaction dependent on
the addition of synthetic U7 RNA that is assembled into a
ribonucleoprotein particle by protein components available in the
extract. In addition to reconstituted U7 snRNP, Xenopus
hairpin-binding protein SLBP1 is necessary for efficient processing.
Histone RNA 3' processing is not affected by addition of
non-destructible cyclin B, which drives the egg extract into M phase,
but SLBP1 is phosphorylated in this extract. SPH-1, the
Xenopus homologue of human p80-coilin found in coiled bodies, is associated with U7 snRNPs. However, this does not depend on
the U7 RNA being able to process histone RNA and also occurs with U1
snRNPs; therefore, association of SPH1 cannot be considered as a
hallmark of a functional U7 snRNP.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) Z71188 and U75681 (hairpin-binding protein sequences).
Assembly of U7 Small Nuclear Ribonucleoprotein Particle and
Histone RNA 3' Processing in Xenopus Egg Extracts*
§¶,, and
Abteilung Entwicklungsbiologie, Zoologisches
Institut, Universität Bern, Baltzerstrasse 4, CH 3012 Bern,
Switzerland, the § Department of Molecular and Cell Biology,
Institute of Medical Sciences, Foresterhill, Aberdeen AB25 2ZD,
Scotland, United Kingdom, and the Medical Research
Council Protein Phosphorylation Unit, Department of
Biochemistry, The University of Dundee, Medical Sciences Institute,
Dundee DD1 4HN, Scotland, United Kingdom
*
This work was supported by the Swiss National Science
Foundation (SNSF) (Grant 31-52619.97 to B. M. and D. Schümperli), the State of Bern (to B. M.), the University of
Aberdeen (to B. M.), the Medical Research Council (to C. S.), the
Association for International Cancer Research (to C. S.), and the
British Council/SNSF joint program (to B. M.and C. S.).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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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