Title |
Implications of Streptomyces coelicolor RraAS1 as an activator of ribonuclease activity of Escherichia coli RNase E |
Author |
Jihune Heo, Sojin Seo, Boeun Lee, Ji-Hyun Yeom, and Kangseok Lee* |
Address |
Department of Life Science, Chung-Ang University, Seoul 06974, Republic of Korea |
Bibliography |
Korean Journal of Microbiology, 52(3),243-248, 2016 |
DOI |
http://dx.doi.org/10.7845/kjm.2016.6047
|
Key Words |
Streptomyces coelicolor, RNase E, RNase ES, RraA, RraAS1 |
Abstract |
RNase E (Rne) is an essential enzyme involved in the processing and degradation of a large portion of RNAs in Escherichia
coli. The enzymatic activity of RNase E is controlled by regulators of ribonuclease activity, namely, RraA and RraB. Gram-positive
bacterium Streptomyces coelicolor also contains homologs of Rne and RraA, designated as RNase ES (Rns), RraAS1, and RraAS2. In the
present study, we investigated the effect of S. coelicolor RraAS1 on the ribonucleolytic activity of RNase E in E. coli. Coexpression of
RraAS1 with Rne resulted in the decreased levels of rpsO, ftsZ, and rnhB mRNAs, which are RNase E substrates, and augmented the
toxic effect of Rne overexpression on cell growth. These in vivo effects appeared to be induced by the binding of RraAS1 to Rne, as
indicated by the results of co-immunoprecipitation analysis. These results suggested that RraAS1 induces ribonucleolytic activity of
RNase E in E. coli. |
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52(3)_01_p.243-248.pdf |