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Consequences of RNase E scarcity in Escherichia coli
Author(s) -
Jain Chaitanya,
Deana Atilio,
Belasco Joel G.
Publication year - 2002
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.1365-2958.2002.02808.x
Subject(s) - endoribonuclease , rnase p , biology , escherichia coli , degradosome , rna , rnase mrp , rnase ph , overproduction , gene , microbiology and biotechnology , biochemistry
Summary The endoribonuclease RNase E plays an important role in RNA processing and degradation in Escherichia coli . The construction of an E. coli strain in which the cellular concentration of RNase E can be precisely controlled has made it possible to examine and quantify the effect of RNase E scarcity on RNA decay, gene regulation and cell growth. These studies show that RNase E participates in a step in the degradation of its RNA substrates that is partially or fully rate‐determining. Our data also indicate that E. coli growth requires a cellular RNase E concentration at least 10–20% of normal and that the feedback mecha‐nism that limits overproduction of RNase E is also able to increase its synthesis when its concentration drops below normal. The magnitude of the in‐crease in RNA longevity under conditions of RNase E scarcity may be limited by an alternative pathway for RNA degradation. Additional experiments show that RNase E is a stable protein in E. coli . No other E. coli gene product, when either mutated or cloned on a multicopy plasmid, seems to be capable of compensating for an inadequate supply of this essential protein.