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Structural and Organizational Studies of Soluble Tar-Chewchea Complexes by Electron Microscopy and Image Analysis

Published online by Cambridge University Press:  02 July 2020

Noreen R. Francis ,
Tanvir R. Shaikh ,
Mikhail N. Levit ,
Linda A. Melanson ,
Jeffrey B. Stock  and
David J. DeRosier
Noreen R. Francis
Affiliation:
The W.M. Keck Institute of Cellular Visualization, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA02454
Tanvir R. Shaikh
Affiliation:
The W.M. Keck Institute of Cellular Visualization, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA02454
Mikhail N. Levit
Affiliation:
Department of Molecular Biology, Princeton University, Princeton, NJ08540
Linda A. Melanson
Affiliation:
The W.M. Keck Institute of Cellular Visualization, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA02454
Jeffrey B. Stock
Affiliation:
Department of Molecular Biology, Princeton University, Princeton, NJ08540
David J. DeRosier
Affiliation:
The W.M. Keck Institute of Cellular Visualization, Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA02454
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Extract

The transmembrane receptor for aspartate, Tar, in Escherichia coliand Salmonellais representative of a large class of receptors that generates chemotaxis responses by regulating the activity of an associated histidine kinase, CheA. Tar is composed of an Nterminal extracellular ligand-binding domain linked through a transmembrane sequence to a C-terminal signaling domain in the cytoplasm. The isolated cytoplasmic domain of Tar fused to a leucine zipper sequence forms soluble ternary complexes with CheA and an adapter protein, CheW. The isolated complex is biochemically active, has a molecular weight of 1,400,000 Daltons, and includes approximately 28 receptor signaling domains for 2 CheA dimers.

Electron microscopy of the complexes indicates well-defined bundles, presumably composed of numerous receptor filaments surrounding a core of CheA dimers and CheW. CheA also interacts with CheY, the response regulator of the bacterial flagellar motor. Immunoelectron microscopy has provided a general picture of the domain organization of the complexes.

Type
Structural Approaches to the Study of Cell Cell Interactions In Three Dimensions
Information
Microscopy and Microanalysis , Volume 5 , Issue S2: Proceedings: Microscopy & Microanalysis '99, Microscopy Society of America 57th Annual Meeting, Microbeam Analysis Society 33rd Annual Meeting, Portland, Oregon August 1-5, 1999 , August 1999 , pp. 1032 - 1033
Copyright
Copyright © Microscopy Society of America

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References

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