DOI: 10.1073/pnas.1709075114
论文题名: Paradoxical enhancement of chemoreceptor detection sensitivity by a sensory adaptation enzyme
作者: Lai R.-Z. ; Han X.-S. ; Dahlquist F.W. ; Parkinson J.S.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2017
卷: 114, 期: 36 起始页码: E7583
结束页码: E7591
语种: 英语
英文关键词: Bacterial chemotaxis
; Dynamic-bundle model
; Nonequilibrium mechanism
; Receptor methyltransferase
; Signaling conformation
Scopus关键词: CheB enzyme
; CheR enzyme
; methyltransferase
; pentapeptide
; unclassified drug
; bacterial protein
; CheB protein, Bacteria
; CheR protein, E coli
; Escherichia coli protein
; ligand
; membrane protein
; methyltransferase
; serine
; adaptation
; Article
; bacterial cell
; carboxy terminal sequence
; chemoreceptor
; chemotaxis
; controlled study
; crystal structure
; enzyme activity
; enzyme conformation
; Escherichia coli K 12
; feedback system
; hydrogen bond
; nonhuman
; priority journal
; quantitative analysis
; receptor binding
; receptor sensitivity
; Salmonella enterica serovar Typhimurium
; signal transduction
; stimulus response
; stoichiometry
; adaptation
; catalysis
; chemoreceptor cell
; Escherichia coli
; metabolism
; physiology
; Adaptation, Biological
; Bacterial Proteins
; Catalysis
; Chemoreceptor Cells
; Escherichia coli
; Escherichia coli Proteins
; Ligands
; Membrane Proteins
; Methyltransferases
; Serine
; Signal Transduction
英文摘要: A sensory adaptation system that tunes chemoreceptor sensitivity enables motile Escherichia coli cells to track chemical gradients with high sensitivity over a wide dynamic range. Sensory adaptation involves feedback control of covalent receptor modifications by two enzymes: CheR, a methyltransferase, and CheB, a methylesterase. This study describes a CheR function that opposes the signaling consequences of its catalytic activity. In the presence of CheR, a variety of mutant serine chemoreceptors displayed up to 40-fold enhanced detection sensitivity to chemoeffector stimuli. This response enhancement effect did not require the known catalytic activity of CheR, but did involve a binding interaction between CheR and receptor molecules. Response enhancement was maximal at low CheR:receptor stoichiometry and quantitative analyses argued against a reversible binding interaction that simply shifts the ON–OFF equilibrium of receptor signaling complexes. Rather, a short-lived CheR binding interaction appears to promote a long-lasting change in receptor molecules, either a covalent modification or conformation that enhances their response to attractant ligands. © 2017, National Academy of Sciences. All rights reserved. Citation statistics:
资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163802
Appears in Collections: 气候变化与战略
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作者单位: Lai, R.-Z., Biology Department, University of Utah, Salt Lake City, UT 84112, United States; Han, X.-S., Biology Department, University of Utah, Salt Lake City, UT 84112, United States; Dahlquist, F.W., Department of Chemistry and Biochemistry, University of California, Santa Barbara, CA 93106, United States; Parkinson, J.S., Biology Department, University of Utah, Salt Lake City, UT 84112, United States
Recommended Citation:
Lai R.-Z.,Han X.-S.,Dahlquist F.W.,et al. Paradoxical enhancement of chemoreceptor detection sensitivity by a sensory adaptation enzyme[J]. Proceedings of the National Academy of Sciences of the United States of America,2017-01-01,114(36)