期刊
STRUCTURE
卷 21, 期 9, 页码 1590-1601出版社
CELL PRESS
DOI: 10.1016/j.str.2013.06.024
关键词
-
资金
- 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
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据