Journal
STRUCTURE
Volume 21, Issue 9, Pages 1590-1601Publisher
CELL PRESS
DOI: 10.1016/j.str.2013.06.024
Keywords
-
Funding
- DOE Office of Biological and Environmental Research
- NIH NIGMS [P41GM103393]
- NCRR [P41RR001209]
- NIH [R01 GM51426, R01 GM32506]
- NIH postdoctoral fellowships [F32 A1082915, F32 GM099173]
- Jane Coffin Childs Memorial Fund
- NIH NIGMS Protein Structure Initiative grant [U54 GM094586]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0923679] Funding Source: National Science Foundation
Ask authors/readers for more resources
Vital to bacterial survival is the faithful propagation of cellular signals, and in Caulobacter crescentus, ChpT is an essential mediator within the cell-cycle circuit. ChpT functions as a histidine-containing phosphotransfer protein (HPt) that shuttles a phosphoryl group from the receiver domain of CckA, the upstream hybrid histidine kinase (HK), to one of two downstream response regulators (CtrA or CpdR) that controls cell-cycle progression. To understand how ChpT interacts with multiple signaling partners, we solved the crystal structure of ChpT at 2.3 angstrom resolution. ChpT adopts a pseudo-HK architecture but does not bind ATP. We identified two point mutation classes affecting phosphotransfer and cell morphology: one that globally impairs ChpT phosphotransfer, and a second that mediates partner selection. Importantly, a small set of conserved ChpT residues promotes signaling crosstalk and contributes to the branched signaling that activates the master regulator CtrA while inactivating the CtrA degradation signal, CpdR.
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