Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM. / Briegel, Ariane; Ortega, Davi R; Mann, Petra; Kjær, Andreas; Ringgaard, Simon; Jensen, Grant J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 113, No. 37, 13.09.2016, p. 10412-7.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Briegel, A, Ortega, DR, Mann, P, Kjær, A, Ringgaard, S & Jensen, GJ 2016, 'Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM', Proceedings of the National Academy of Sciences of the United States of America, vol. 113, no. 37, pp. 10412-7. https://doi.org/10.1073/pnas.1604693113

APA

Briegel, A., Ortega, D. R., Mann, P., Kjær, A., Ringgaard, S., & Jensen, G. J. (2016). Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM. Proceedings of the National Academy of Sciences of the United States of America, 113(37), 10412-7. https://doi.org/10.1073/pnas.1604693113

Vancouver

Briegel A, Ortega DR, Mann P, Kjær A, Ringgaard S, Jensen GJ. Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM. Proceedings of the National Academy of Sciences of the United States of America. 2016 Sep 13;113(37):10412-7. https://doi.org/10.1073/pnas.1604693113

Author

Briegel, Ariane ; Ortega, Davi R ; Mann, Petra ; Kjær, Andreas ; Ringgaard, Simon ; Jensen, Grant J. / Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM. In: Proceedings of the National Academy of Sciences of the United States of America. 2016 ; Vol. 113, No. 37. pp. 10412-7.

Bibtex

@article{1140580611374cdc84ccdbd656c760c3,
title = "Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM",
abstract = "Nearly all motile bacterial cells use a highly sensitive and adaptable sensory system to detect changes in nutrient concentrations in the environment and guide their movements toward attractants and away from repellents. The best-studied bacterial chemoreceptor arrays are membrane-bound. Many motile bacteria contain one or more additional, sometimes purely cytoplasmic, chemoreceptor systems. Vibrio cholerae contains three chemotaxis clusters (I, II, and III). Here, using electron cryotomography, we explore V. cholerae's cytoplasmic chemoreceptor array and establish that it is formed by proteins from cluster I. We further identify a chemoreceptor with an unusual domain architecture, DosM, which is essential for formation of the cytoplasmic arrays. DosM contains two signaling domains and spans the two-layered cytoplasmic arrays. Finally, we present evidence suggesting that this type of receptor is important for the structural stability of the cytoplasmic array.",
keywords = "Journal Article",
author = "Ariane Briegel and Ortega, {Davi R} and Petra Mann and Andreas Kj{\ae}r and Simon Ringgaard and Jensen, {Grant J}",
year = "2016",
month = sep,
day = "13",
doi = "10.1073/pnas.1604693113",
language = "English",
volume = "113",
pages = "10412--7",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "37",

}

RIS

TY - JOUR

T1 - Chemotaxis cluster 1 proteins form cytoplasmic arrays in Vibrio cholerae and are stabilized by a double signaling domain receptor DosM

AU - Briegel, Ariane

AU - Ortega, Davi R

AU - Mann, Petra

AU - Kjær, Andreas

AU - Ringgaard, Simon

AU - Jensen, Grant J

PY - 2016/9/13

Y1 - 2016/9/13

N2 - Nearly all motile bacterial cells use a highly sensitive and adaptable sensory system to detect changes in nutrient concentrations in the environment and guide their movements toward attractants and away from repellents. The best-studied bacterial chemoreceptor arrays are membrane-bound. Many motile bacteria contain one or more additional, sometimes purely cytoplasmic, chemoreceptor systems. Vibrio cholerae contains three chemotaxis clusters (I, II, and III). Here, using electron cryotomography, we explore V. cholerae's cytoplasmic chemoreceptor array and establish that it is formed by proteins from cluster I. We further identify a chemoreceptor with an unusual domain architecture, DosM, which is essential for formation of the cytoplasmic arrays. DosM contains two signaling domains and spans the two-layered cytoplasmic arrays. Finally, we present evidence suggesting that this type of receptor is important for the structural stability of the cytoplasmic array.

AB - Nearly all motile bacterial cells use a highly sensitive and adaptable sensory system to detect changes in nutrient concentrations in the environment and guide their movements toward attractants and away from repellents. The best-studied bacterial chemoreceptor arrays are membrane-bound. Many motile bacteria contain one or more additional, sometimes purely cytoplasmic, chemoreceptor systems. Vibrio cholerae contains three chemotaxis clusters (I, II, and III). Here, using electron cryotomography, we explore V. cholerae's cytoplasmic chemoreceptor array and establish that it is formed by proteins from cluster I. We further identify a chemoreceptor with an unusual domain architecture, DosM, which is essential for formation of the cytoplasmic arrays. DosM contains two signaling domains and spans the two-layered cytoplasmic arrays. Finally, we present evidence suggesting that this type of receptor is important for the structural stability of the cytoplasmic array.

KW - Journal Article

U2 - 10.1073/pnas.1604693113

DO - 10.1073/pnas.1604693113

M3 - Journal article

C2 - 27573843

VL - 113

SP - 10412

EP - 10417

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 37

ER -

ID: 179169064