H. Pluk et al., CDNA CLONING AND CHARACTERIZATION OF THE HUMAN U3 SMALL NUCLEOLAR RIBONUCLEOPROTEIN COMPLEX-ASSOCIATED 55-KILODALTON PROTEIN, Molecular and cellular biology, 18(1), 1998, pp. 488-498
The eukaryotic nucleolus contains a large number of small RNA molecule
s (snoRNAs) which, in the form of small nucleolar ribonucleoprotein co
mplexes (snoRNPs), are involved in the processing and modification of
pre-rRNA. The most abundant and one of the best-conserved snoRNAs is t
he U3 RNA. So far, only one human U3 snoRNA-associated protein, fibril
larin, has been characterized. Previously, the U3 snoRNPwas purified f
rom CHO cells, and three proteins of 15, 50, and 55 kDa were found to
copurify with the U3 snoRNA (B. Lubben, C. Marshallsay, N. Rottmann, a
nd R. Luhrmann, Nucleic Acids Res. 21:5377-5385, 1993). Here we report
the cDNA cloning and characterization of the human U3 snoRNP-associat
ed 55-kDa protein, The isolated cDNA codes for a novel nucleolar prote
in which is specifically associated with the U3 snoRNA. This protein,
referred to as hU3-55k, is the first characterized U3 snoRNP-specific
protein from humans. hU3-55k is a new member of the family of WD-40 re
peat proteins and is conserved throughout evolution. It appears that t
he C-terminal end of hU3-55k is required for nucleolar localization an
d U3 snoRNA binding.