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A developmentally regulated Streptomyces endoribonuclease resembles ribonuclease E of Escherichia coli
Author(s) -
Hagège Juliette M.,
Cohen Stanley N.
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1997.5311904.x
Subject(s) - biology , endoribonuclease , rnase mrp , rnase p , rnase ph , streptomyces coelicolor , microbiology and biotechnology , rna , streptomyces , escherichia coli , ribonuclease iii , biochemistry , genetics , bacteria , gene , rna interference
We report that the Streptomyces species S. lividans and S. coelicolor , morphologically complex Gram‐positive soil bacteria, contain a developmentally regulated endoribonuclease activity (here named RNase ES) that functionally and immunologically resembles Escherichia coli RNase E. In Streptomyces cells, RNA I — the antisense repressor of replication of ColE1‐type plasmids — is cleaved at sites attacked by RNase E. A Mg 2+ ‐dependent endonuclease that produces RNase E‐like cleavages in RNA I and 9S ribosomal RNA was identified in S. lividans cell extracts. A Streptomyces peptide migrating at 70 kDa in SDS/polyacrylamide gels binds to RNase E substrates and reacts with three separate anti‐RNase E monoclonal antibodies; the endonucleolytic cleavage activity co‐purified with the immunoreactive 70 kDa peptide. We show that RNase ES activity is regulated during the Streptomyces life cycle: activity increased as cells progressed from exponential growth to stationary phase in liquid culture, or from mycelial growth to sporulation on solid media. While mutations that interfere with S. coelicolor development late in its life cycle did not prevent this developmentally associated increase in RNase ES activity, the increase was blocked by a mutation ( bldA ) that interferes early with both morphological and physiological differentiation.