Nucleic Acids Research, Vol 26, Issue 19 4508-4515, Copyright © 1998 by Oxford University Press
RS Savkur and MO Olson
Protein B23 is an abundant nucleolar protein and a putative ribosome
assembly factor which possesses an intrinsic ribonuclease activity. In the
current work, the effects of RNA sequence and secondary structure on the
cleavage preference by protein B23 were studied. Protein B23 ribonuclease
preferentially cleaved the single-stranded homopolymers poly(A), poly(U)
and poly(C). However, double-stranded co-polymers and poly(G) were
resistant to cleavage. No base specificity was observed with an
oligoribonucleotide substrate. The action of protein B23 ribonuclease on
different regions of pre-rRNA was studied using transcripts synthesized in
vitro from cloned rDNA segments. Although no specific cleavages were
detected in transcripts containing sequences from the 5' external
transcribed spacer or the first internal transcribed spacer, the enzyme
preferentially cleaved the second internal transcribed spacer (ITS2)
approximately 250 nt downstream from the 3'-end of 5.8S rRNA. Preferential
cleavage was retained when the transcript was extended by 100 nt at the
3'-end, but abolished in a transcript lacking this cleavage site.
Furthermore, this site was not susceptible to cleavage by RNase A or RNase
T1. These results, in conjunction with the sub-nucleolar localization of
the protein with elements of the processing machinery, suggest that the
protein B23 endoribonuclease could play a role in pre-rRNA processing in
ITS2.
ARTICLES
Preferential cleavage in pre-ribosomal RNA byprotein B23 endoribonuclease
Department of Biochemistry, The University of Mississippi Medical Center, 2500 North State Street, Jackson, MS 39216-4505, USA.
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