A chemoreceptor from Pseudomonas putida forms active signalling complexes in Escherichia coli
Chemoreceptors sense environmental stimuli and transmit the information to the flagellar motors via a histidine kinase that controls the phosphorylation level of the effector protein CheY. The cytoplasmic domain of chemoreceptors consists of a long α-helical hairpin that forms, in the dimer, a coile...
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Published in | Microbiology (Society for General Microbiology) Vol. 158; no. 9; pp. 2283 - 2292 |
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Main Authors | , , |
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01.09.2012
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Abstract | Chemoreceptors sense environmental stimuli and transmit the information to the flagellar motors via a histidine kinase that controls the phosphorylation level of the effector protein CheY. The cytoplasmic domain of chemoreceptors consists of a long α-helical hairpin that forms, in the dimer, a coiled-coil four-helix bundle. Even though the sequence and general structure of the cytoplasmic domain are strongly conserved within Eubacteria and Archaea, the total length of the α-helical hairpin is variable and defines seven classes of chemoreceptors. In this work we assessed the functional properties of a Pseudomonas receptor when assembled in signalling complexes with Escherichia coli proteins. Our results show that the foreign receptor does not confer fully chemotactic abilities upon E. coli cells, but is able to form active ternary complexes that respond to the specific stimuli by modulating the activity of the associated kinase. The observed responses are subject to adaptation, depending on the presence of the methylation enzymes CheR and/or CheB. The ability of foreign receptors to signal through signalling complexes with non-cognate proteins would allow the use of the well-studied E. coli system to reveal the detection specificity of uncharacterized chemoreceptors from other micro-organisms. |
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AbstractList | Chemoreceptors sense environmental stimuli and transmit the information to the flagellar motors via a histidine kinase that controls the phosphorylation level of the effector protein CheY. The cytoplasmic domain of chemoreceptors consists of a long α-helical hairpin that forms, in the dimer, a coiled-coil four-helix bundle. Even though the sequence and general structure of the cytoplasmic domain are strongly conserved within Eubacteria and Archaea, the total length of the α-helical hairpin is variable and defines seven classes of chemoreceptors. In this work we assessed the functional properties of a Pseudomonas receptor when assembled in signalling complexes with Escherichia coli proteins. Our results show that the foreign receptor does not confer fully chemotactic abilities upon E. coli cells, but is able to form active ternary complexes that respond to the specific stimuli by modulating the activity of the associated kinase. The observed responses are subject to adaptation, depending on the presence of the methylation enzymes CheR and/or CheB. The ability of foreign receptors to signal through signalling complexes with non-cognate proteins would allow the use of the well-studied E. coli system to reveal the detection specificity of uncharacterized chemoreceptors from other micro-organisms. Chemoreceptors sense environmental stimuli and transmit the information to the flagellar motors via a histidine kinase that controls the phosphorylation level of the effector protein CheY. The cytoplasmic domain of chemoreceptors consists of a long α-helical hairpin that forms, in the dimer, a coiled-coil four-helix bundle. Even though the sequence and general structure of the cytoplasmic domain are strongly conserved within Eubacteria and Archaea, the total length of the α-helical hairpin is variable and defines seven classes of chemoreceptors. In this work we assessed the functional properties of a Pseudomonas receptor when assembled in signalling complexes with Escherichia coli proteins. Our results show that the foreign receptor does not confer fully chemotactic abilities upon E. coli cells, but is able to form active ternary complexes that respond to the specific stimuli by modulating the activity of the associated kinase. The observed responses are subject to adaptation, depending on the presence of the methylation enzymes CheR and/or CheB. The ability of foreign receptors to signal through signalling complexes with non-cognate proteins would allow the use of the well-studied E. coli system to reveal the detection specificity of uncharacterized chemoreceptors from other micro-organisms.Chemoreceptors sense environmental stimuli and transmit the information to the flagellar motors via a histidine kinase that controls the phosphorylation level of the effector protein CheY. The cytoplasmic domain of chemoreceptors consists of a long α-helical hairpin that forms, in the dimer, a coiled-coil four-helix bundle. Even though the sequence and general structure of the cytoplasmic domain are strongly conserved within Eubacteria and Archaea, the total length of the α-helical hairpin is variable and defines seven classes of chemoreceptors. In this work we assessed the functional properties of a Pseudomonas receptor when assembled in signalling complexes with Escherichia coli proteins. Our results show that the foreign receptor does not confer fully chemotactic abilities upon E. coli cells, but is able to form active ternary complexes that respond to the specific stimuli by modulating the activity of the associated kinase. The observed responses are subject to adaptation, depending on the presence of the methylation enzymes CheR and/or CheB. The ability of foreign receptors to signal through signalling complexes with non-cognate proteins would allow the use of the well-studied E. coli system to reveal the detection specificity of uncharacterized chemoreceptors from other micro-organisms. |
Author | Studdert, Claudia A. Herrera Seitz, M. Karina Soto, Débora |
Author_xml | – sequence: 1 givenname: M. Karina surname: Herrera Seitz fullname: Herrera Seitz, M. Karina organization: Instituto de Investigaciones Biológicas, Universidad Nacional de Mar del Plata, Mar del Plata, Buenos Aires, Argentina – sequence: 2 givenname: Débora surname: Soto fullname: Soto, Débora organization: Instituto de Investigaciones Biológicas, Universidad Nacional de Mar del Plata, Mar del Plata, Buenos Aires, Argentina – sequence: 3 givenname: Claudia A. surname: Studdert fullname: Studdert, Claudia A. organization: Instituto de Investigaciones Biológicas, Universidad Nacional de Mar del Plata, Mar del Plata, Buenos Aires, Argentina |
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Cites_doi | 10.1099/00221287-143-10-3223 10.1038/23512 10.1038/nsmb1085 10.1073/pnas.0905181106 10.1128/JB.151.1.106-113.1982 10.1371/journal.pone.0018184 10.1128/jb.176.20.6340-6348.1994 10.1038/227680a0 10.1016/j.mib.2009.12.014 10.1073/pnas.0609359104 10.1128/JB.185.2.544-552.2003 10.1126/scisignal.2000724 10.1111/j.1574-6968.1997.tb12738.x 10.1111/j.1365-2958.2011.07928.x 10.1128/JB.185.7.2354-2361.2003 10.1128/JB.134.3.1141-1156.1978 10.1073/pnas.0506040102 10.1073/pnas.1115719109 10.1046/j.1365-2958.1997.3241682.x 10.1016/S0021-9258(18)32536-5 10.1111/j.1365-2958.2009.06770.x 10.1046/j.1462-2920.2002.00366.x 10.1073/pnas.0308622100 10.1016/0378-1119(77)90000-2 10.1128/JB.126.2.758-770.1976 10.1073/pnas.092071899 10.1128/JB.186.12.3730-3737.2004 10.1111/j.1365-2958.2010.07477.x 10.1111/j.1462-2920.2010.02325.x 10.1046/j.1365-2958.2000.02044.x |
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Keywords | Pseudomonadales Escherichia coli Bacteria Pseudomonadaceae Pseudomonas putida Chemoreceptor Enterobacteriaceae |
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SubjectTerms | Bacteriology Biological and medical sciences Escherichia coli - genetics Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Gene Expression Genetic Engineering - methods Microbiology Miscellaneous Pseudomonas putida - genetics Pseudomonas putida - metabolism Recombinant Proteins - genetics Recombinant Proteins - metabolism Recombination, Genetic Signal Transduction |
Title | A chemoreceptor from Pseudomonas putida forms active signalling complexes in Escherichia coli |
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