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Vol. 11, Issue 4, 1153-1167, April 2000
Division of Cell Biology, German Cancer Research Center, D-69120
Heidelberg, Germany
We report the identification, cDNA cloning, and molecular
characterization of a novel, constitutive nucleolar protein. The cDNA-deduced amino acid sequence of the human protein defines a
polypeptide of a calculated mass of 61.5 kDa and an isoelectric point
of 9.9. Inspection of the primary sequence disclosed that the protein
is a member of the family of "DEAD-box" proteins, representing a
subgroup of putative ATP-dependent RNA helicases. ATPase activity of
the recombinant protein is evident and stimulated by a variety of
polynucleotides tested. Immunolocalization studies revealed that
protein NOH61 (nucleolar helicase of 61 kDa) is highly conserved during
evolution and shows a strong accumulation in nucleoli. Biochemical
experiments have shown that protein NOH61 synthesized in vitro
sediments with ~11.5 S, i.e., apparently as homo-oligomeric
structures. By contrast, sucrose gradient centrifugation analysis of
cellular extracts obtained with buffers of elevated ionic strength (600 mM NaCl) revealed that the solubilized native protein sediments with
~4 S, suggestive of the monomeric form. Interestingly, protein NOH61
has also been identified as a specific constituent of free
nucleoplasmic 65S preribosomal particles but is absent from cytoplasmic
ribosomes. Treatment of cultured cells with 1) the transcription
inhibitor actinomycin D and 2) RNase A results in a complete
dissociation of NOH61 from nucleolar structures. The specific
intracellular localization and its striking sequence homology to other
known RNA helicases lead to the hypothesis that protein NOH61 might be
involved in ribosome synthesis, most likely during the assembly process
of the large (60S) ribosomal subunit.
Corresponding author. E-mail address:
M.Schmidt-Zachmann{at}dkfz-heidelberg.de.
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