A mutational wrench in the HAMP gearbox
Article first published online: 12 AUG 2009
© 2009 Blackwell Publishing Ltd
Volume 73, Issue 5, pages 742–746, September 2009
How to Cite
Manson, M. D. (2009), A mutational wrench in the HAMP gearbox. Molecular Microbiology, 73: 742–746. doi: 10.1111/j.1365-2958.2009.06818.x
- Issue published online: 24 AUG 2009
- Article first published online: 12 AUG 2009
- Accepted 21 July, 2009.
HAMP domains communicate between input and output signalling elements in bacterial proteins. In the Tsr chemoreceptor, they convert axial movement of transmembrane helix 2 into changes in packing of the cytoplasmic kinase-control module (KCM). Zhou et al. suggest transmembrane helix 2 ‘tugs’ on HAMP to destabilize x-da packing of the parallel four-helix bundle of the HAMP homodimer. Attractants would inhibit tugging. HAMP stability may be inversely related to stability of the a-d packing of the anti-parallel four-helix bundle of KCM, a relationship possibly facilitated by HAMP/KCM helical mismatch. The beauty of this idea lies in its simplicity and testability.