Publication Date:
2015-11-29
Description:
Publication date: Available online 27 November 2015 Source: FEBS Letters Author(s): Inas Al-Younis, Aloysius Wong, Chris Gehring Adenylate Cyclases (ACs) catalyze the formation of the second messenger cyclic adenosine 3′, 5′-monophosphate (cAMP) from adenosine 5’-triphosphate (ATP). Although cAMP is increasingly recognized as an important signaling 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 AtKUP7 1-100 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 AtKUP7 1-100 generates cAMP in vitro .
Print ISSN:
0014-5793
Electronic ISSN:
1873-3468
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
