Processing of the rne transcript by an RNase E-independent amino acid-dependent mechanism.

The Journal of Biological Chemistry
W M Woo, S Lin-Chao

Abstract

RNase E is encoded by the rne (also known as ams or hmp) gene and is the principal enzyme that controls the chemical decay of bulk mRNA in Escherichia coli. Earlier work has shown that RNase E degrades its own mRNA, autoregulating production of the RNase E protein. Here we show that in cells lacking RNase E activity, the 3.6-kilobase rne gene transcript is cleaved site specifically at two locations near its center by a novel endonuclease whose activity is modulated by the presence or absence of amino acids in the culture medium. These cleavages produce a 2-kilobase RNase E-sensitive RNA fragment corresponding to the 3' half of the transcript. Using primer extension and RNase protection analysis, we mapped RNase E-independent cleavages to sites 1558 and 1576 nucleotides from the 5' end of the rne transcript (coordinates 1738 and 1747 of the rne gene). Our results indicate the existence of a previously unknown RNase E-independent mechanism for degradation of rne transcripts and further demonstrate that this mechanism responds to changes in cell growth conditions.

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Citations

Jun 17, 1999·FEMS Microbiology Reviews·A W Nicholson
Oct 27, 1999·Proceedings of the National Academy of Sciences of the United States of America·S Lin-ChaoY T Lin
May 20, 2015·Biochimica Et Biophysica Acta·Razika HusseinHan N Lim

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