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J. Biol. Chem., Vol. 278, Issue 4, 2147-2156, January 24, 2003
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From the Wellcome Trust Centre for Cell Biology, Swann Building,
King's Buildings, University of Edinburgh, Edinburgh EH9 3JR,
United Kingdom
Depletion of any of the essential Lsm
proteins, Lsm2-5p or Lsm8p, delayed pre-rRNA processing and led
to the accumulation of many aberrant processing intermediates,
indicating that an Lsm complex is required to maintain the normally
strict order of processing events. In addition, high levels of
degradation products derived from both precursors and mature rRNAs
accumulated in Lsm-depleted strains. Depletion of the essential Lsm
proteins reduced the apparent processivity of both 5' and 3'
exonuclease activities involved in 5.8S rRNA processing, and the
degradation intermediates that accumulated were consistent with
inefficient 5' and 3' degradation. Many, but not all, pre-rRNA species
could be coprecipitated with tagged Lsm3p, but not with tagged Lsm1p or
non-tagged control strains, suggesting their direct interaction with an
Lsm2-8p complex. We propose that Lsm proteins facilitate RNA protein
interactions and structural changes required during ribosomal subunit assembly.
Lsm Proteins Are Required for Normal Processing and Stability of
Ribosomal RNAs*
,
*
This work was supported by the Wellcome Trust.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: Institut de Biologie Moleculaire et
Cellulaire, UPR 9002 du CNRS, 15, rue R. Descartes, 67084 Strasbourg Cedex, France.
§
To whom correspondence should be addressed. Tel.: 44-131-650-7092;
Fax: 44-131-650-7040; E-mail: d.tollervey@ed.ac.uk.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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