Specificity of the BvgAS and EvgAS phosphorelay is mediated by the C-terminal HPt domains of the sensor proteins

Molecular Microbiology
A L PerraudR Gross

Abstract

Despite the presence of highly conserved signalling modules, significant cross-communication between different two-component systems has only rarely been observed. Domain swapping and the characterization of liberated signalling modules enabled us to characterize in vitro the protein domains that mediate specificity and are responsible for the high fidelity in the phosphorelay of the unorthodox Bvg and Evg two-component systems. Under equimolar conditions, significant in vitro phosphorylation of purified BvgA and EvgA proteins was only obtained by their histidine kinases, BvgS and EvgS respectively. One hybrid histidine kinase consisting of the BvgS transmitter and HPt domains and of the EvgS receiver domain (BvgS-TO-EvgS-R) was able to phosphorylate BvgA but not EvgA. In contrast, the hybrid protein consisting of the BvgS transmitter and the EvgS receiver and HPt domains (BvgS-T-EvgS-RO) was unable to phosphorylate BvgA but efficiently phosphorylated EvgA. These results demonstrate that the C-terminal HPt domains of the sensor proteins endow the unorthodox two-component systems with a high specificity for the corresponding regulator protein. In the case of the response regulators, the receiver but not the output domains contri...Continue Reading

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Citations

May 29, 2000·Biochimica Et Biophysica Acta·A L PerraudR Gross
Aug 14, 2003·Trends in Microbiology·Jetta J E Bijlsma, Eduardo A Groisman
Sep 22, 2010·Proceedings of the National Academy of Sciences of the United States of America·Julien HerrouFrançoise Jacob-Dubuisson
Feb 26, 2009·The Journal of Biological Chemistry·Andreas BuschTino Krell
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Feb 17, 2006·Current Opinion in Microbiology·Dagmar Beier, Roy Gross
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Jun 8, 2021·Frontiers in Microbiology·Shinya InadaYoko Eguchi
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Dec 9, 2000·International Journal of Medical Microbiology : IJMM·M BantscheffR Gross

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