CaltechAUTHORS
  A Caltech Library Service

Universal architecture of bacterial chemoreceptor arrays

Briegel, Ariane and Ortega, Davi R. and Tocheva, Elitza I. and Wuichet, Kristin and Li, Zhuo and Chen, Songye and Müller, Axel and Iancu, Cristina V. and Murphy, Gavin E. and Dobro, Megan J. and Zhulin, Igor B. and Jensen, Grant J. (2009) Universal architecture of bacterial chemoreceptor arrays. Proceedings of the National Academy of Sciences of the United States of America, 106 (40). pp. 17181-17186. ISSN 0027-8424. PMCID PMC2761316. https://resolver.caltech.edu/CaltechAUTHORS:20091019-151620276

[img]
Preview
PDF - Published Version
See Usage Policy.

3168Kb
[img]
Preview
PDF - Supplemental Material
See Usage Policy.

9Mb
[img]
Preview
PDF - Supplemental Material
See Usage Policy.

701Kb

Use this Persistent URL to link to this item: https://resolver.caltech.edu/CaltechAUTHORS:20091019-151620276

Abstract

Chemoreceptors are key components of the high-performance signal transduction system that controls bacterial chemotaxis. Chemoreceptors are typically localized in a cluster at the cell pole, where interactions among the receptors in the cluster are thought to contribute to the high sensitivity, wide dynamic range, and precise adaptation of the signaling system. Previous structural and genomic studies have produced conflicting models, however, for the arrangement of the chemoreceptors in the clusters. Using whole-cell electron cryo-tomography, here we show that chemoreceptors of different classes and in many different species representing several major bacterial phyla are all arranged into a highly conserved, 12-nm hexagonal array consistent with the proposed “trimer of dimers” organization. The various observed lengths of the receptors confirm current models for the methylation, flexible bundle, signaling, and linker sub-domains in vivo. Our results suggest that the basic mechanism and function of receptor clustering is universal among bacterial species and was thus conserved during evolution.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1073/pnas.0905181106DOIArticle
http://www.pnas.org/cgi/content/full/0905181106/DCSupplementalPublisherSupporting Information
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2761316/PubMed CentralArticle
ORCID:
AuthorORCID
Briegel, Ariane0000-0003-3733-3725
Ortega, Davi R.0000-0002-8344-2335
Tocheva, Elitza I.0000-0002-4869-8319
Chen, Songye0000-0001-5407-5049
Iancu, Cristina V.0000-0002-7352-9226
Dobro, Megan J.0000-0002-6464-3932
Zhulin, Igor B.0000-0002-6708-5323
Jensen, Grant J.0000-0003-1556-4864
Additional Information:© 2009 National Academy of Sciences. Edited by Laura L. Kiessling, University of Wisconsin, Madison, WI, and approved July 20, 2009 (received for review May 11, 2009). Author contributions: A.B. and G.J.J. designed research; A.B., D.R.O., E.I.T., K.W., Z.L., S.C., A.M., C.V.I., G.E.M., and M.J.D. performed research; A.B., D.R.O., E.I.T., K.W., and I.B.Z. analyzed data; and A.B., D.R.O., E.I.T., I.B.Z., and G.J.J. wrote the paper. The authors wish to thank Eric Matson, Reinhard Rachel, Kevin Bruhn, Gordon Cannon, Alan Barbour, Sarkis Mazmanian, Jeanette Beatty, Maria Sandkvist, Dianne Newman, and John S. Parkinson for bacterial strains; Howard Berg for the penicillin treatment protocol for E. coli; Jane H. Ding for computational support; Juergen Plitzko, Alasdair McDowall and Jian Shi for EM support; and Roger Alexander, Luke Ulrich, and Bhanu Rekapalli for assistance and helpful suggestions. The authors also thank Professor Wolfgang Baumeister (Max Planck Institute for Biochemistry, Martinsried, Germany) for the permission to include the data from T. maritima (which was collected in his laboratory and under his supervision) in this study. This work was supported in part by National Institutes of Health Grants R01 AI067548 and P50 GM082545 (to G.J.J.) and R01 GM72285 (to I.B.Z.), as well as the Howard Hughes Medical Institute, the Beckman Institute at Caltech, and gifts to Caltech from the Gordon and Betty Moore Foundation and Agouron Institute.
Funders:
Funding AgencyGrant Number
NIHR01 AI067548
NIHP50 GM082545
NIHR01 GM72285
Howard Hughes Medical Institute (HHMI)UNSPECIFIED
Caltech Beckman InstituteUNSPECIFIED
Gordon and Betty Moore FoundationUNSPECIFIED
Agouron InstituteUNSPECIFIED
Subject Keywords:bacterial ultrastructure; chemotaxis; electron cryo-tomography
Issue or Number:40
PubMed Central ID:PMC2761316
Record Number:CaltechAUTHORS:20091019-151620276
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20091019-151620276
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:16387
Collection:CaltechAUTHORS
Deposited By: Jason Perez
Deposited On:20 Oct 2009 20:29
Last Modified:24 Apr 2020 19:15

Repository Staff Only: item control page