TITLE

The global regulator RNase III modulates translation repression by the transcription elongation factor N

AUTHOR(S)
Wilson, Helen R.; Daiguan Yu; Peters, III., Howard K.; Jian-guang Zhou; Court, Donald L.
PUB. DATE
August 2002
SOURCE
EMBO Journal;8/1/2002, Vol. 21 Issue 15, p4154
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
Efficient expression of most bacteriophage &lamda; early genes depends upon the formation of an antiterminating transcription complex to overcome transcription terminators in the early operons, PL and PR. Formation of this complex requires the phage-encoded protein N, the first gene product expressed from the PL operon. The N leader RNA contains, in this order: the NUTL site, an RNase III-sensitive hairpin and the N ribosome-binding site. N bound to NUTL RNA is part of both the antitermination complex and an auto-regulatory complex that represses the translation of the N gene. In this study, we show that cleavage of the N leader by RNase III does not inhibit antitermination but prevents N-mediated translation repression of N gene expression. In fact, by preventing N auto- regulation, RNase III activates N gene translation at least 200-fold. N-mediated translation repression is extremely sensitive to growth rate, reflecting the growth rate regulation of RNase III expression itself. Given N protein's critical role in &lamda; development, the level of RNase III activity therefore serves as an important sensor of physiological conditions for the bacteriophage.
ACCESSION #
12956017

 

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