Nucleic Acids Research, Vol 24, Issue 7 1246-1251, Copyright © 1996 by Oxford University Press
R Rauhut, A Jager, C Conrad and G Klug
The large subunit ribosomal RNA of the purple bacterium Rhodobacter
capsulatus shows fragmentation into pieces of 14 and 16S, both fragments
forming the functional equivalent of intact 23S rRNA. An RNA- processing
step removes an extra stem-loop structure from the 23S rRNA [Kordes, E.,
Jock, S., Fritsch, J., Bosch, F. and Klug, G. (1994) J. Bacteriol., 176,
1121-1127]. Taking advantage of the fragmentation deficient mutant strain
Fm65, we used genetic complementation to find the mutated gene responsible
for this aberration. It was identified as the Rhodobacter homologue to mc
from Escherichia coli encoding endoribonuclease III (RNase III). The
predicted protein has 226 amino acids with a molecular weight of 25.5 kDa.
It shares high homology with other known RNase III enzymes over the full
length. In particular it shows the double-stranded RNA-binding domain
(dsRBD) motif essential for binding of dsRNA substrates. The Fm65 mutant
has a frame shift mutation resulting in complete loss of the dsRBD
rendering the enzyme inactive. The cloned Rhodobacter enzyme can substitute
RNase III activity in an RNase III deficient E. coli strain. Contrary to E.
coli, the Rhodobacter mc is in one operon together with the lep gene
encoding the leader peptidase.
ARTICLES
Identification and analysis of the rnc gene for RNase III in Rhodobacter capsulatus
Institut fur Mikrobiologie und Molekularbiologie der Justus Liebig Universitat Giessen, Germany.
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