Zobrazeno 1 - 10
of 102
pro vyhledávání: '"Gerald L. Hazelbauer"'
Publikováno v:
mBio, Vol 12, Iss 6 (2021)
ABSTRACT Methylesterase/deamidase CheB is a key component of bacterial chemotaxis systems. It is also a prominent example of a two-component response regulator in which the effector domain is an enzyme. Like other response regulators, CheB is activat
Externí odkaz:
https://doaj.org/article/16a1ce51ec9d4923847b9f6a5fad1498
Publikováno v:
PLoS Computational Biology, Vol 14, Iss 7, p e1006305 (2018)
It is challenging to decipher molecular mechanisms in biological systems from system-level input-output data, especially for complex processes that involve interactions among multiple components. We addressed this general problem for the bacterial hi
Externí odkaz:
https://doaj.org/article/22a81f82c7a342b9b827c23ca949373c
Autor:
Gabriela S. Schlau-Cohen, Mikaila C Hoffman, Julianne M Troiano, Jesse B. Gordon, Mingshan Li, Gerald L. Hazelbauer
Publikováno v:
ACS Chem Biol
Transmembrane receptors are central components of the chemosensory systems by which motile bacteria detect and respond to chemical gradients. An attractant bound to the receptor periplasmic domain generates conformational signals that regulate a hist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8521971a070cdc00aac009e83a45c5e
https://doi.org/10.1021/acschembio.1c00576
https://doi.org/10.1021/acschembio.1c00576
Publikováno v:
mBio, Vol 12, Iss 6 (2021)
mBio
mBio
Methylesterase/deamidase CheB is a key component of bacterial chemotaxis systems. It is also a prominent example of a two-component response regulator in which the effector domain is an enzyme. Like other response regulators, CheB is activated by pho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4ff0d4da0b8564ef353f9adc2dd4c15
https://doi.org/10.1128/mbio.03106-21
https://doi.org/10.1128/mbio.03106-21
Autor:
Gerald L. Hazelbauer, Mingshan Li
Publikováno v:
Protein Sci
Methylation of specific chemoreceptor glutamyl residues by methyltransferase CheR mediates sensory adaptation and gradient sensing in bacterial chemotaxis. Enzyme action is a function of chemoreceptor signaling conformation: kinase‐off receptors ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20fd1685ac477b3434d87fb07e449be6
https://doi.org/10.1002/pro.3760
https://doi.org/10.1002/pro.3760
Publikováno v:
J Bacteriol
In bacterial chemotaxis, chemoreceptors in signaling complexes modulate the activity of two-component histidine kinase CheA in response to chemical stimuli. CheA catalyzes phosphoryl transfer from ATP to a histidinyl residue of its P1 domain. That ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a15855fc7eaba05a508f57f24d04262
https://pubmed.ncbi.nlm.nih.gov/32341073
https://pubmed.ncbi.nlm.nih.gov/32341073
Publikováno v:
Protein Science. 26:1535-1546
Autophosphorylating histidine kinase CheA is central to signaling in bacterial chemotaxis. The kinase donates its phosphoryl group to two response regulators, CheY that controls flagellar rotation and thus motility and CheB, crucial for sensory adapt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::df41454ad33a37c2e30c4e8cd2d1721a
https://doi.org/10.1002/pro.3179
https://doi.org/10.1002/pro.3179
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 12, p 2989 (2019)
International Journal of Molecular Sciences
Volume 20
Issue 12
International Journal of Molecular Sciences
Volume 20
Issue 12
The chemotactic sensory system enables motile bacteria to move toward favorable environments. Throughout bacterial diversity, the chemoreceptors that mediate chemotaxis are clustered into densely packed arrays of signaling complexes. In these arrays,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72147b3b28297e26ff6a60dd80c5211c
https://www.mdpi.com/1422-0067/20/12/2989
https://www.mdpi.com/1422-0067/20/12/2989
Publikováno v:
Protein Science. 24:1764-1776
Cytoplasmic domains of transmembrane bacterial chemoreceptors are largely extended four-helix coiled coils. Previous observations suggested the domain was structurally dynamic. We probed directly backbone dynamics of this domain of the transmembrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40c67b38cfc92e9a4c4a076836ac3ac1
https://doi.org/10.1002/pro.2767
https://doi.org/10.1002/pro.2767
Publikováno v:
Trends in Microbiology. 23:257-266
Motile Escherichia coli cells track gradients of attractant and repellent chemicals in their environment with transmembrane chemoreceptor proteins. These receptors operate in cooperative arrays to produce large changes in the activity of a signaling
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e21bf21ec306eedd971e3a68ffbfa3c
https://doi.org/10.1016/j.tim.2015.03.003
https://doi.org/10.1016/j.tim.2015.03.003