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Journal of Bacteriology, March 2009, p. 1765-1776, Vol. 191, No. 6
0021-9193/09/$08.00+0     doi:10.1128/JB.01405-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The Atypical Hybrid Histidine Protein Kinase RodK in Myxococcus xanthus: Spatial Proximity Supersedes Kinetic Preference in Phosphotransfer Reactions{triangledown} ,{dagger}

Sigrun Wegener-Feldbrügge and Lotte Søgaard-Andersen*

Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Str., 35043 Marburg, Germany

Received 7 October 2008/ Accepted 5 January 2009

Many proteins of two-component signal transduction systems (TCS) have domain structures that do not comply with a phosphate flow as observed in linear TCS, phosphorelays, or simple branched pathways. An example is RodK, which is essential for fruiting body formation in Myxococcus xanthus and, in addition to a sensor domain, consists of a kinase domain and three receiver domains (RodK-R1, -R2, and -R3), all of which are functionally important. We identified the RokA response regulator as part of the RodK pathway. In vitro the isolated RodK kinase domain engages in phosphotransfer to RodK-R3 and RokA, with a kinetic preference for RokA. However, in the context of the full-length protein, the RodK kinase domain has a preference for phosphotransfer to RodK-R3 over RokA. We suggest that in full-length RodK, the spatial proximity of the RodK kinase domain and RodK-R3 compensate for the kinetic preference of the isolated kinase domain for RokA. Thus, the kinetic preference observed using an isolated kinase domain of a hybrid kinase does not necessarily reflect the phosphotransfer preference of the full-length protein. We speculate that the phosphorylation status of RodK-R1 and RodK-R2 determines whether RodK engages in phosphotransfer to RodK-R3 or RokA in vivo.

* Corresponding author. Mailing address: Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Str., 35043 Marburg, Germany. Phone: 49-6421-178201. Fax: 49-6421-178209. E-mail: sogaard{at}mpi-marburg.mpg.de

{triangledown} Published ahead of print on 9 January 2009.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, March 2009, p. 1765-1776, Vol. 191, No. 6
0021-9193/09/$08.00+0     doi:10.1128/JB.01405-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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