Prof Mike Merrick
Throughout my research career my interests have focussed on bacterial nitrogen metabolism and the ways in which bacteria control all aspects of that metabolism in response to the availability of fixed nitrogen (for reviews see: Arcondeguy et al, 2001; Huergo et al, 2013).
For many years the primary focus of research in my lab concerned the biology of the ubiquitous ammonium transport (Amt) proteins and of the signal transduction proteins of the PII family. Ammonium transport (Amt) proteins are found in eubacteria, archaebacteria, fungi, plants, and lower animals. Members of the Amt family are also present in higher animals including humans where their homologues are the Rhesus (Rh) proteins. The PII proteins are one of the most widely distributed families of signal transduction proteins in nature. They are pivotal players in the control of nitrogen metabolism and are found in bacteria, archaea and in the plastids of plants. A detailed discussion of these topics can be found on my personal web pages.
JIC-led studentship programme receives £12.5M investment for next generation of scientistsread more
Proceedings of the National Academy of Sciences of the United States of America 110 (32) p12948-12953
Publisher’s version: 10.1073/pnas.1304386110
Journal of Biological Chemistry 285 (40) p31037-31045
Publisher’s version: 10.1074/jbc.M110.153908
Frontiers in Microbiology 5 p763
Publisher’s version: 10.3389/fmicb.2014.00763
Association and dissociation of the GlnK-AmtB complex in response to cellular nitrogen status can occur in the absence of GlnK post-translational modification
Frontiers in Microbiology 5 p731
Publisher’s version: 10.3389/fmicb.2014.00731
Ammonium transport proteins with changes in one of the conserved pore histidines have different performance in ammonia and methylamine conduction.
PLoS ONE (5)
Publisher’s version: 10.1371/journal.pone.0062745
FEMS Microbiology Reviews 37 p251-283
Publisher’s version: 10.1111/j.1574-6976.2012.00351.x
PII signal transduction proteins: pivotal players in post-translational control of nitrogenase activity.
Microbiology 158 (Pt 1) p176-190
Publisher’s version: 10.1099/mic.0.049783-0
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