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J. Biol. Chem., Vol. 262, Issue 23, 10922-10925, Aug, 1987
B Bugler, H Bourbon, B Lapeyre, MO Wallace, JH Chang, F Amalric and MO Olson
Nucleolin (C23 or 100 kDa) is a major nucleolar phosphoprotein whose
primary structure has recently been determined (Lapeyre, B., Bourbon, H.,
and Amalric, F. (1987) Proc. Natl. Acad. Sci. U. S. A. 84, 1472- 1476) and
found to be associated with preribosomal RNA (Herrera, A. H., and Olson, M.
O. J. (1986) Biochemistry 25, 6258-6263). To identify the RNA binding
region of the molecule, cyanogen bromide fragments were tested for binding
of 18 S and 28 S ribosomal RNA by a "Western blotting" technique. Fragments
with apparent molecular masses of 13, 33, and 47 kDa bound RNA with no
preference for either 18 S or 28 S RNA. By protein sequencing, these
fragments were localized in the carboxyl-terminal two-thirds of the
molecule. The nucleolin sequence was searched for the ribonucleoprotein
consensus sequence found in other RNA binding proteins. Four copies of a
closely related 11-residue sequence were found within 80-90 residue repeats
in the RNA binding region between residues 285 and 629. These results
suggest that a highly conserved structure for the binding of different
classes of RNA is utilized by several proteins.
RNA binding fragments from nucleolin contain the ribonucleoprotein consensus sequence
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