The Arabidopsis thalianaK+-uptake permease 7 (AtKUP7) contains a functional cytosolic adenylate cyclase catalytic centre

Handle URI:
http://hdl.handle.net/10754/621444
Title:
The Arabidopsis thalianaK+-uptake permease 7 (AtKUP7) contains a functional cytosolic adenylate cyclase catalytic centre
Authors:
Al-Younis, Inas; Wong, Aloysius Tze ( 0000-0002-9105-5845 ) ; Gehring, Christoph A. ( 0000-0003-4355-4591 )
Abstract:
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 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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division
Citation:
Al-Younis I, Wong A, Gehring C (2015) TheArabidopsis thalianaK+-uptake permease 7 (AtKUP7) contains a functional cytosolic adenylate cyclase catalytic centre. FEBS Letters 589: 3848–3852. Available: http://dx.doi.org/10.1016/j.febslet.2015.11.038.
Publisher:
Wiley-Blackwell
Journal:
FEBS Letters
Issue Date:
27-Nov-2015
DOI:
10.1016/j.febslet.2015.11.038
Type:
Article
ISSN:
0014-5793
Sponsors:
This project was funded by King Abdullah University of Science and Technology.
Appears in Collections:
Articles; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorAl-Younis, Inasen
dc.contributor.authorWong, Aloysius Tzeen
dc.contributor.authorGehring, Christoph A.en
dc.date.accessioned2016-11-03T08:29:27Z-
dc.date.available2016-11-03T08:29:27Z-
dc.date.issued2015-11-27en
dc.identifier.citationAl-Younis I, Wong A, Gehring C (2015) TheArabidopsis thalianaK+-uptake permease 7 (AtKUP7) contains a functional cytosolic adenylate cyclase catalytic centre. FEBS Letters 589: 3848–3852. Available: http://dx.doi.org/10.1016/j.febslet.2015.11.038.en
dc.identifier.issn0014-5793en
dc.identifier.doi10.1016/j.febslet.2015.11.038en
dc.identifier.urihttp://hdl.handle.net/10754/621444-
dc.description.abstractAdenylate 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 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.en
dc.description.sponsorshipThis project was funded by King Abdullah University of Science and Technology.en
dc.publisherWiley-Blackwellen
dc.subjectcAMPen
dc.subjectAdenylate cyclaseen
dc.subjectSecond messengeren
dc.subjectArabidopsis thalianaen
dc.titleThe Arabidopsis thalianaK+-uptake permease 7 (AtKUP7) contains a functional cytosolic adenylate cyclase catalytic centreen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.identifier.journalFEBS Lettersen
kaust.authorAl-Younis, Inasen
kaust.authorWong, Aloysius Tzeen
kaust.authorGehring, Christoph A.en
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