The Arabidopsis thaliana K+-Uptake Permease 5 (AtKUP5) Contains a Functional Cytosolic Adenylate Cyclase Essential for K+ Transport

Al-Younis, Inas; Wong, Aloysius; Lemtiri‐Chlieh, Fouad; Schmöckel, Sandra M.; Tester, Mark; Gehring, Chris; Donaldson, Lara

doi:10.3389/fpls.2018.01645

Cited by 49 publications

(63 citation statements)

References 92 publications

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“…Indeed, there have been well-characterized examples in receptor protein complexes such as BRI1 from Arabidopsis thaliana where externally located hormone recognition domain is connected via a transmembrane region to a cytoplasmic canonical kinase domain that also accommodates a smaller moonlighting guanylate cyclase (GC) center (14). The same is also observed in Arabidopsis potassium transporter and channel (KUP5 and GORK) proteins, where moonlighting adenylate cyclase (AC) center and ABA binding site were found to occupy cytosolic sites of these multi-pass membrane proteins (15, 16). This complexity also makes it incredibly difficult to examine precise cellular regulatory functions of individual components and their broader biological roles.…”

Section: Introductionsupporting

confidence: 55%

PlantMP: a database for moonlighting plant proteins

Qian

et al. 2019

Database

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Moonlighting proteins are single polypeptide chains capable of executing two or more distinct biochemical and/or biological functions. Here, we describe the development of PlantMP, which is a manually curated online-based database of plant proteins that are known to `moonlight’. The database contains searchable UniProt IDs and names, canonical and moonlighting functions, gene ontology numbers, plant species as well as links to the PubMed indexed articles. Proteins homologous to experimentally confirmed moonlighting proteins from the model plant Arabidopsis thaliana are provided as a separate list of `likely moonlighters’. Additionally, we also provide a list of predicted Arabidopsis moonlighting proteins reported in the literature. Currently, PlantMP contains 110 plant moonlighting proteins, 10 `likely moonlighters’ and 27 `predicted moonlighters’. Organizing plant moonlighting proteins in one platform enables researchers to conveniently harvest plant-specific raw and processed data such as the molecular functions, biological roles and structural features essential for hypothesis formulation in basic research and for biotechnological innovations.

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Section: Introductionsupporting

confidence: 55%

PlantMP: a database for moonlighting plant proteins

Qian

et al. 2019

Database

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“…However, such centers may be identified in proteins by applying search motifs (terms) that are built based on consensus amino acids in annotated and experimentally-confirmed proteins across species [17,18]. This approach has been successfully applied for the discovery of plant guanylate cyclases (GCs) and adenylate cyclases (ACs), which cannot be identified by querying, e.g., the Arabidopsis proteome with annotated GCs or ACs from animals, fungi, or bacteria [19,20,21,22,23,24,25,26]. This search method has also enabled the discovery of an abscisic acid (ABA) binding site in an Arabidopsis guard cell outward rectifying K + channel (GORK) that has subsequently been shown to be directly modulated by ABA [27].…”

Section: Resultsmentioning

confidence: 99%

Discovery of a Nitric Oxide-Responsive Protein in Arabidopsis thaliana

et al. 2019

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In plants, much like in animals, nitric oxide (NO) has been established as an important gaseous signaling molecule. However, contrary to animal systems, NO-sensitive or NO-responsive proteins that bind NO in the form of a sensor or participating in redox reactions have remained elusive. Here, we applied a search term constructed based on conserved and functionally annotated amino acids at the centers of Heme Nitric Oxide/Oxygen (H-NOX) domains in annotated and experimentally-tested gas-binding proteins from lower and higher eukaryotes, in order to identify candidate NO-binding proteins in Arabidopsis thaliana. The selection of candidate NO-binding proteins identified from the motif search was supported by structural modeling. This approach identified AtLRB3 (At4g01160), a member of the Light Response Bric-a-Brac/Tramtrack/Broad Complex (BTB) family, as a candidate NO-binding protein. AtLRB3 was heterologously expressed and purified, and then tested for NO-response. Spectroscopic data confirmed that AtLRB3 contains a histidine-ligated heme cofactor and importantly, the addition of NO to AtLRB3 yielded absorption characteristics reminiscent of canonical H-NOX proteins. Furthermore, substitution of the heme iron-coordinating histidine at the H-NOX center with a leucine strongly impaired the NO-response. Our finding therefore established AtLRB3 as a NO-interacting protein and future characterizations will focus on resolving the nature of this response.

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“…This is likely to be similar in plant ACs, whereby AC domains coexist and cofunction with other domains. Few ACs known for this include a class III AC protein (MpCAPE) in the liverwort, Marchantia polymorpha , with phosphodiesterase activity at its N-terminus end (Kasahara et al, 2016) and two Arabidopsis proteins, AtKUP5 and AtKUP7, with K + -uptake permease activity (Al-Younis et al, 2015, 2018).…”

Section: Introductionmentioning

confidence: 99%

New Perspectives on Plant Adenylyl Cyclases

Ruzvidzo

Gehring

Wong

2019

Front. Mol. Biosci.

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It is increasingly clear that plant genomes encode numerous complex multidomain proteins that harbor functional adenylyl cyclase (AC) centers. These AC containing proteins have well-documented roles in development and responses to the environment. However, it is only for a few of these proteins that we are beginning to understand the intramolecular mechanisms that govern their cellular and biological functions, as detailed characterizations are biochemically and structurally challenging given that these poorly conserved AC centers typically constitute only a small fraction (<10%) of complex plant proteins. Here, we offer fresh perspectives on their seemingly cryptic activities specifically showing evidence for the presence of multiple functional AC centers in a single protein and linking their catalytic strengths to the Mg2+/Mn2+-binding amino acids. We used a previously described computational approach to identify candidate multidomain proteins from Arabidopsis thaliana that contain multiple AC centers and show, using an Arabidopsis leucine-rich repeat containing protein (TAIR ID: At3g14460; AtLRRAC1) as example, biochemical evidence for multienzymatic activities. Importantly, all AC-containing fragments of this protein can complement the AC-deficient mutant cyaA in Escherichia coli, while structural modeling coupled with molecular docking simulations supports catalytic feasibility albeit to varying degrees as determined by the frequency of suitable substrate binding poses predicted for the AC sites. This statistic correlates well with the enzymatic assays, which implied that the greatly reduced AC activities is due to the absence of the negatively charged [DE] amino acids previously assigned to cation-, in particular Mg2+/Mn2+-binding roles in ACs.

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The Arabidopsis thaliana K+-Uptake Permease 5 (AtKUP5) Contains a Functional Cytosolic Adenylate Cyclase Essential for K+ Transport

Cited by 49 publications

References 92 publications

PlantMP: a database for moonlighting plant proteins

PlantMP: a database for moonlighting plant proteins

Discovery of a Nitric Oxide-Responsive Protein in Arabidopsis thaliana

New Perspectives on Plant Adenylyl Cyclases

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