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dc.contributor.authorMarondedze, Claudiusen_US
dc.contributor.authorWong, Aloysiusen_US
dc.contributor.authorThomas, Ludivineen_US
dc.contributor.authorIrving, Helenen_US
dc.contributor.authorGehring, Chrisen_US
dc.identifier.citationMarondedze, C., Wong, A., Thomas, L., Irving, H., & Gehring, C. (2015). Cyclic nucleotide monophosphates in plants and plant signaling. In Non-canonical Cyclic Nucleotides (pp. 87-103). Springer, Cham.en_US
dc.description.abstractCyclic nucleotide monophosphates (cNMPs) and the enzymes that can generate them are of increasing interest in the plant sciences. Arguably, the major recent advance came with the release of the complete Arabidopsis thaliana genome that has enabled the systematic search for adenylate (ACs) or guanylate cyclases (GCs) and did eventually lead to the discovery of a number of GCs in higher plants. Many of these proteins have complex domain architectures with AC or GC centers moonlighting within cytosolic kinase domains. Recent reports indicated the presence of not just the canonical cNMPs (i.e., cAMP and cGMP), but also the noncanonical cCMP, cUMP, cIMP, and cdTMP in plant tissues, and this raises several questions. Firstly, what are the functions of these cNMPs, and, secondly, which enzymes can convert the substrate triphosphates into the respective noncanonical cNMPs? The first question is addressed here by comparing the reactive oxygen species (ROS) response of cAMP and cGMP to that elicited by the noncanonical cCMP or cIMP. The results show that particularly cIMP can induce significant ROS production. To answer, at least in part, the second question, we have evaluated homology models of experimentally confirmed plant GCs probing the substrate specificity by molecular docking simulations to determine if they can conceivably catalytically convert substrates other than ATP or GTP. In summary, molecular modeling and substrate docking simulations can contribute to the evaluation of cyclases for noncanonical cyclic mononucleotides and thereby further our understanding of the molecular mechanism that underlie cNMP-dependent signaling in planta.en_US
dc.format.extent17 pagesen_US
dc.publisherCham, Switzerland: Springeren_US
dc.relation.ispartofNon-canonical Cyclic Nucleotidesen_US
dc.subject.lcshAdenylate Cyclaseen_US
dc.subject.lcshArabidopsis Thalianaen_US
dc.subject.lcshGuanylate Cyclaseen_US
dc.titleCyclic nucleotide monophosphates in plants and plant signalingen_US
dc.typeBook Chapteren_US
dc.rights.licenseAttribution-NonCommercial 4.0 International (CC BY-NC 4.0)en_US
dc.subject.keywordsCyclic Nucleotide Monophosphatesen_US
dc.subject.keywordsSecond Messengeren_US
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