PII proteins are one of the most widely distributed signal transduction proteins in Nature, being ubiquitous in bacteria, archaea and plants. They act by protein–protein interaction to control the activities of a wide range of enzymes, transcription factors and transport proteins, the great majority of which are involved in cellular nitrogen metabolism. The regulatory activities of PII proteins are mediated through their ability to bind the key effector metabolites 2-OG (2-oxoglutarate), ATP and ADP. However, the molecular basis of these regulatory effects remains unclear. Recent advances in the solution of the crystal structures of PII proteins complexed with some of their target proteins, as well as the identification of the ATP/ADP- and 2-OG-binding sites, have improved our understanding of their mode of action. In all of the complex structures solved to date, the flexible T-loops of PII facilitate interaction with the target protein. The effector molecules appear to play a key role in modulating the conformation of the T-loops and thereby regulating the interactions between PII and its targets.
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Conference Article|
January 19 2011
The role of effector molecules in signal transduction by PII proteins
Martha Radchenko;
Martha Radchenko
1Department of Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, U.K.
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Mike Merrick
Mike Merrick
1
1Department of Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, U.K.
1To whom correspondence should be addressed (email mike.merrick@bbsrc.ac.uk).
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Publisher: Portland Press Ltd
Received:
August 31 2010
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (1): 189–194.
Article history
Received:
August 31 2010
Citation
Martha Radchenko, Mike Merrick; The role of effector molecules in signal transduction by PII proteins. Biochem Soc Trans 1 February 2011; 39 (1): 189–194. doi: https://doi.org/10.1042/BST0390189
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