Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8383977 | FEBS Letters | 2015 | 5 Pages |
Abstract
Adenylate cyclases (ACs) catalyse the formation of the second messenger cyclic adenosine 3â²,5â²-monophosphate (cAMP) from adenosine 5â²-triphosphate (ATP). Although cAMP is increasingly recognised as an important signalling molecule in higher plants, ACs have remained somewhat elusive. Here we used a search motif derived from experimentally tested guanylyl cyclases (GCs), substituted the residues essential for substrate specificity and identified the Arabidopsis thaliana K+-uptake permease 7 (AtKUP7) as one of several candidate ACs. Firstly, we show that a recombinant N-terminal, cytosolic domain of AtKUP71-100 is able to complement the AC-deficient mutant cyaA in Escherichia coli and thus restoring the fermentation of lactose, and secondly, we demonstrate with both enzyme immunoassays and mass spectrometry that a recombinant AtKUP71-100 generates cAMP in vitro.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Inas Al-Younis, Aloysius Wong, Chris Gehring,