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Vol. 11, Issue 2, 567-577, February 2000
i
, and
*Department of Anatomy and Structural Biology, Albert Einstein
College of Medicine, Bronx, New York 10461; and Small nucleolar ribonucleoprotein particles (snoRNPs) mainly
catalyze the modification of rRNA. The two major classes of snoRNPs, box H/ACA and box C/D, function in the pseudouridylation and
2'-O-methylation, respectively, of specific nucleotides.
The emerging view based on studies in yeast is that each class of
snoRNPs is composed of a unique set of proteins. Here we present a
characterization of mammalian snoRNPs. We show that the previously
characterized NAP57 is specific for box H/ACA snoRNPs, whereas the
newly identified NAP65, the rat homologue of yeast Nop5/58p, is a
component of the box C/D class. Using coimmunoprecipitation
experiments, we show that the nucleolar and coiled-body protein Nopp140
interacts with both classes of snoRNPs. This interaction is
corroborated in vivo by the exclusive depletion of snoRNP proteins from
nucleoli in cells transfected with a dominant negative Nopp140
construct. Interestingly, RNA polymerase I transcription is arrested in
nucleoli depleted of snoRNPs, raising the possibility of a feedback
mechanism between rRNA modification and transcription. Moreover, the
Nopp140-snoRNP interaction appears to be conserved in yeast, because
depletion of Srp40p, the yeast Nopp140 homologue, in a conditional
lethal strain induces the loss of box H/ACA small nucleolar RNAs. We propose that Nopp140 functions as a chaperone of snoRNPs in yeast and
vertebrate cells.
Friedrich
Miescher Institute, 4058 Basel, Switzerland
Present address: Department of Therapeutic
Radiology, Yale University School of Medicine, New Haven, CT 06520.
§
Corresponding author. E-mail address:
meier{at}aecom.yu.edu.
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