Journal
GENES & DEVELOPMENT
Volume 21, Issue 1, Pages 124-136Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/gad.1496707
Keywords
sigma(E); stress response; proteolysis; ATP-dependent proteases; DegS; RseP
Categories
Funding
- NIGMS NIH HHS [R01 GM049224, GM-049224, GM-32678, R01 GM049224-15] Funding Source: Medline
Ask authors/readers for more resources
Proteolytic cascades often transduce signals between cellular compartments, but the features of these cascades that permit efficient conversion of a biological signal into a transcriptional output are not well elucidated. sigma(E) mediates an envelope stress response in Escherichia coli, and its activity is controlled by regulated degradation of RseA, a membrane-spanning anti-sigma factor. Examination of the individual steps in this protease cascade reveals that the initial, signal-sensing cleavage step is rate-limiting; that multiple ATP-dependent proteases degrade the cytoplasmic fragment of RseA and that dissociation of sigma(E) from RseA is so slow that most free sigma(E) must be generated by the active degradation of RseA. As a consequence, the degradation rate of RseA is set by the amount of inducing signal, and insulated from the load on and activity of the cytoplasmic proteases. Additionally, changes in RseA degradation rate are rapidly reflected in altered sigma E activity. These design features are attractive as general components of signal transduction pathways governed by unstable negative regulators.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available