Suppression of cell-cell variation by cooperative interaction of phosphatase and response regulator.

Xiang Liu, Rongjing Zhang, Junhua Yuan

Abstract read

In one paragraph

Article in Biophysical journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Xiang LiuHefei National Laboratory for Physical Sciences at the Microscale and Department of Physics, University of Science and Technology of China, Hefei, Anhui, China.

Rongjing ZhangHefei National Laboratory for Physical Sciences at the Microscale and Department of Physics, University of Science and Technology of China, Hefei, Anhui, China. Electronic address: rjzhang@ustc.edu.cn.

Junhua YuanHefei National Laboratory for Physical Sciences at the Microscale and Department of Physics, University of Science and Technology of China, Hefei, Anhui, China. Electronic address: jhyuan@ustc.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In bacterial chemotaxis, the output of chemosensing, the concentration of the response regulator CheY-P that was constantly adjusted by the opposing action of the kinase CheA and the phosphatase CheZ, serves as the input of the ultrasensitive flagellar motor that drives bacterial motility. The steady-state kinase activity exhibits large cell-to-cell variation that may result in similar variation in CheY-P concentration. Here, we found that the in vivo phosphatase activity is highly cooperative with respect to CheY-P concentration, and this suppresses the cell-to-cell variation of CheY-P concentration so that it falls within the operational range of the flagellar motor. Therefore, the cooperativity of the CheZ and CheY-P interaction we identified here provided a mechanism of robust coupling between the output of chemosensing and the input of the flagellar motor. Suppression of cell heterogeneity by cooperativity of protein-protein interaction is likely a common feature in many biological signaling systems.

Indexed as

Escherichia coli ProteinsPhosphoric Monoester HydrolasesBacterial ProteinsChemotaxisHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsPhosphorylationBacterial ProteinsEscherichia coli ProteinsHistidine KinaseMembrane ProteinsMethyl-Accepting Chemotaxis ProteinsPhosphoric Monoester Hydrolases

Identifiers

PMID34896368

DOI10.1016/j.bpj.2021.12.012

PMCPMC8790193

What OpenQuestion holds

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.