Document Detail


Isolated bacterial chemosensory array possesses quasi- and ultrastable components: functional links between array stability, cooperativity, and order.
MedLine Citation:
PMID:  23186266     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Bacteria utilize a large multiprotein chemosensory array to sense attractants and repellents in their environment. The array is a hexagonal lattice formed from three core proteins: a transmembrane receptor, the His kinase CheA, and the adaptor protein CheW. The resulting, highly networked array architecture yields several advantages including strong positive cooperativity in the attractant response and rapid signal transduction through the preformed, integrated signaling circuit. Moreover, when isolated from cells or reconstituted in isolated bacterial membranes, the array possesses extreme kinetic stability termed ultrastability (Erbse and Falke (2009) Biochemistry 48:6975-87) and is the most long-lived multiprotein enzyme complex described to date. The isolated array retains kinase activity, attractant regulation, and its bound core proteins for days or more at 22 °C. The present work quantitates this ultrastability and investigates its origin. The results demonstrate that arrays consist of two major components: (i) a quasi-stable component with a lifetime of 1-2 days that decays due to slow proteolysis of CheA kinase in the lattice and (ii) a truly ultrastable component with a lifetime of ~20 days that is substantially more protected from proteolysis. Following proteolysis of the quasi-stable component the apparent positive cooperativity of the array increases, arguing the quasi-stable component is not as cooperative as the ultrastable component. Introduction of structural defects into the array by coupling a bulky probe to a subset of receptors reveals that modification of only 2% of the receptor population is sufficient to abolish ultrastability, supporting the hypothesis that the ultrastable component requires a high level of array spatial order. Overall, the findings are consistent with a model in which the quasi- and ultrastable components arise from distinct regions of the array, such that the ultrastable regions possess more extensive, better-ordered, multivalent interconnectivities between core components, thereby yielding extraordinary stability and cooperativity. Furthermore, the findings indicate that the chemosensory array is a promising platform for the development of ultrastable biosensors.
Authors:
Peter F Slivka; Joseph J Falke
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-12-11
Journal Detail:
Title:  Biochemistry     Volume:  51     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-12-21     Completed Date:  2013-02-19     Revised Date:  2014-01-09    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  10218-28     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Bacterial Outer Membrane Proteins / metabolism
Bacterial Proteins / chemistry*,  genetics
Chemotaxis / physiology
Escherichia coli Proteins / metabolism
Membrane Proteins / chemistry*,  genetics
Multienzyme Complexes / metabolism
Multiprotein Complexes / chemistry*
Mutation
Protein Stability*
Signal Transduction / physiology
Trypsin / metabolism
Grant Support
ID/Acronym/Agency:
R01 GM-040731/GM/NIGMS NIH HHS; R01 GM040731/GM/NIGMS NIH HHS; T32 GM065103/GM/NIGMS NIH HHS; T32 GM065103/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Outer Membrane Proteins; 0/Bacterial Proteins; 0/Escherichia coli Proteins; 0/Membrane Proteins; 0/Multienzyme Complexes; 0/Multiprotein Complexes; 0/methyl-accepting chemotaxis proteins; EC 2.7.3.-/envZ protein, E coli; EC 3.4.21.4/Trypsin
Comments/Corrections

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