Cytokinesis signals truncation of the PodJ polarity factor by a cell cycle-regulated protease

We demonstrate that successive cleavage events involving r egulated i ntramembrane p roteolysis (Rip) occur as a function of time during the Caulobacter cell cycle. The proteolytic substrate PodJ L is a polar factor that recruits proteins required for polar organelle biogenesis to the correct cell p...

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Bibliographic Details
Published in:The EMBO journal 2006-01, Vol.25 (2), p.377-386
Main Authors: Chen, Joseph C, Hottes, Alison K, McAdams, Harley H, McGrath, Patrick T, Viollier, Patrick H, Shapiro, Lucy
Format: Article
Language:English
Subjects:
Bacterial Proteins - metabolism
beta-Galactosidase
Caulobacter
Caulobacter crescentus - physiology
cell division
Cell Polarity - physiology
Cytokinesis - physiology
differentiation
EMBO06
EMBO23
Gene Expression Regulation, Bacterial - physiology
Immunoblotting
Membrane Proteins - metabolism
Membranes
Microarray Analysis
Microscopy, Fluorescence
Peptide Hydrolases - metabolism
Periplasmic Proteins - metabolism
pilus
proteolysis
Signal Transduction - physiology
Substrates
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Summary:We demonstrate that successive cleavage events involving r egulated i ntramembrane p roteolysis (Rip) occur as a function of time during the Caulobacter cell cycle. The proteolytic substrate PodJ L is a polar factor that recruits proteins required for polar organelle biogenesis to the correct cell pole at a defined time in the cell cycle. We have identified a periplasmic protease (PerP) that initiates the proteolytic sequence by truncating PodJ L to a form with altered activity (PodJ S ). Expression of perP is regulated by a signal transduction system that activates cell type‐specific transcription programs and conversion of PodJ L to PodJ S in response to the completion of cytokinesis. PodJ S , sequestered to the progeny swarmer cell, is subsequently released from the polar membrane by the membrane metalloprotease MmpA for degradation during the swarmer‐to‐stalked cell transition. This sequence of proteolytic events contributes to the asymmetric localization of PodJ isoforms to the appropriate cell pole. Thus, temporal activation of the PerP protease and spatial restriction of the polar PodJ L substrate cooperatively control the cell cycle‐dependent onset of Rip.
ISSN:0261-4189
1460-2075
DOI:10.1038/sj.emboj.7600935