Previous Article | Next Article ![]()
J. Bacteriol., 07 1996, 3917-3925, Vol 178, No. 13
M Kido, K Yamanaka, T Mitani, H Niki, T Ogura and S Hiraga
We have isolated suppressor mutants that suppress temperature-sensitive
colony formation and anucleate cell production of a mukB mutation. A
linkage group (smbB) of the suppressor mutations is located in the
rne/ams/hmp gene encoding the processing endoribonuclease RNase E. All of
the rne (smbB) mutants code for truncated RNase E polypeptides lacking a
carboxyl-terminal half. The amount of MukB protein was higher in these rne
mutants than that in the rne+ strain. These rne mutants grew nearly
normally in the mukB+ genetic background. The copy number of plasmid pBR322
in these rne mutants was lower than that in the rne+ isogenic strain. The
results suggest that these rne mutations increase the half-lives of mukB
mRNA and RNAI of pBR322, the antisense RNA regulating ColE1-type plasmid
replication. We have demonstrated that the wild-type RNase E protein bound
to polynucleotide phosphorylase (PNPase) but a truncated RNase E
polypeptide lacking the C-terminal half did not. We conclude that the
C-terminal half of RNase E is not essential for viability but plays an
important role for binding with PNPase. RNase E and PNPase of the
multiprotein complex presumably cooperate for effective processing and
turnover of specific substrates, such as mRNAs and other RNAs in vivo.
Copyright © 1996, American Society for Microbiology
RNase E polypeptides lacking a carboxyl-terminal half suppress a mukB mutation in Escherichia coli
Department of Molecular Cell Biology, Institute of Molecular Embryology and Genetics, Kumamoto University School of Medicine, Kumamoto, Japan.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»