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J. Biol. Chem., Vol. 275, Issue 47, 36957-36965, November 24, 2000
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From the Department of Structural Biology, Isis Pharmaceuticals,
Carlsbad, California 92008
A human RNase III gene encodes a protein of 160 kDa with multiple domains, a proline-rich, a serine- and arginine-rich,
and an RNase III domain. The expressed purified RNase III domain
cleaves double-strand RNA and does not cleave single-strand RNA. The
gene is ubiquitously expressed in human tissues and cell lines, and the
protein is localized in the nucleus of the cell. The levels of
transcription and translation of the protein do not change during
different phases of the cell cycle. However, a significant fraction of
the protein in the nucleus is translocated to the nucleolus during the
S phase of the cell cycle. That this human RNase III is involved in
processing of pre-rRNA, but might cleave at sites different from those
described for yeast RNase III, is shown by antisense inhibition of
RNase III expression. Inhibition of human RNase III expression causes
cell death, suggesting an essential role for human RNase III in the
cell. The antisense inhibition technique used in this study provides an
effective method for functional analysis of newly identified human genes.
Human RNase III Is a 160-kDa Protein Involved in Preribosomal
RNA Processing*
,,
*
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.
Contributed equally to the results of this work.
§
To whom correspondence should be addressed: Dept. of Structural
Biology, Isis Pharmaceuticals, 2292 Faraday Ave., Carlsbad, CA 92008. Tel.: 760-603-2301; Fax: 760-931-0265; E-mail:
scrooke@isisph.com.
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