Conserved small non-coding RNAs that belong to the σE regulon:: Role in down-regulation of outer membrane proteins
Conserved small non-coding RNAs that belong to the σE regulon:: Role in down-regulation of outer membrane proteins
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DOI:
10.1016/j.jmb.2006.09.004
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发表时间:
2006-11-17
影响因子:
5.6
通讯作者:
Valentin-Hansen, Poul
中科院分区:
文献类型:
--
作者:
Johansen, Jesper;Rasmussen, Anders Aamann;Valentin-Hansen, Poul
Enteric bacteria respond to misfolded proteins by activating the transcription of "heat shock" genes. These genes are arranged in two major regulons controlled by the alternative sigma factors sigma(H) and sigma(E). The two transcription factors coordinate the stress response in different cellular compartments; the sigma(H) regulon is induced by stress in the cytoplasm whereas the sigma(E) regulon is activated by stress signals in the cell envelope. In Escherichia coli sigma(E) plays a central role in maintaining cell envelope integrity both under stress conditions and during normal growth. Previous work established that sigma(E) is essential for viability of the bacterium and up-regulates expression of approximately 100 protein-encoding genes that influences nearly every aspect of the cell envelope. Moreover, the expression of several outer membrane proteins is down-regulated upon a activation. Here, we show that two Hfq-binding small RNAs, MicA and RybB, are under positive control of sigma(E). Transient induction of RybB resulted in decreased levels of the mRNAs encoding OmpC and OmpW. sigma(E)-mediated regulation of ompC and ompW expression was abolished in strains lacking RybB or Hfq. Recently MicA was shown to act in destabilizing the ompA transcript when rapidly grown cells entered the stationary phase of growth. Also, the alternative sigma factor down-regulates this message in a small non-coding RNA-dependent fashion. These findings add the sigma(E) regulon to the growing list of stress induced regulatory circuits that include small regulatory RNAs and provide insight in a homeostatic loop that prevent a build-up of unassembled outer membrane proteins in the envelope. (c) 2006 Elsevier Ltd. All rights reserved.