Nucleic Acids Research, Vol 26, Issue 19 4446-4453, Copyright © 1998 by Oxford University Press
C Conrad, R Rauhut and G Klug
23S rRNA in Rhodobacter capsulatus shows endoribonuclease III (RNase
III)-dependent fragmentation in vivo at a unique extra stem-loop extending
from position 1271 to 1331. RNase III is a double strand (ds)- specific
endoribonuclease. This substrate preference is mediated by a
double-stranded RNA binding domain (dsRBD) within the protein. Although a
certain degree of double strandedness is a prerequisite, the question
arises what structural features exactly make this extra stem-loop an RNase
III cleavage site, distinguishing it from the plethora of stem- loops in
23S rRNA? We used RNase III purified from R.capsulatus and Escherichia
coli, respectively, together with well known substrates for E.coli RNase
III and RNA substrates derived from the special cleavage site in
R.capsulatus 23S rRNA to study the interaction between the Rhodobacter
enzyme and the fragmentation site. Although both enzymes are very similar
in their amino acid sequence, they exhibit significant differences in
binding and cleavage of these in vitro substrates.
ARTICLES
Different cleavage specificities of RNases III from Rhodobacter capsulatus and Escherichia coli
Institut fur Mikro- und Molekularbiologie der Justus-Liebig-Universitat Giessen, Frankfurter Strasse 107,35392 Giessen, Germany.
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