PlantMP: a database for moonlighting plant proteins

Abstract

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.

New Perspectives on Plant Adenylyl Cyclases

“…The possibility of proteins harboring multiple catalytically active AC centers is intriguing as it adds yet another layer of complexity to the regulation of signaling pathways in plant cells (Wong et al, 2015; Marondedze et al, 2017; Irving et al, 2018; Kwezi et al, 2018; Swiezawska et al, 2018; Su et al, 2019). Multiple functional AC centers in a single protein may also offer an additive effect which can accumulatively increase the catalytic strength.…”

“…It has been established that cyclic nucleotide monophosphates, cyclic guanosine monophosphate, and cyclic adenosine monophosphate (cAMP), and their generating enzymes, guanylyl cyclases (GCs) and adenylyl cyclases (ACs), play critical roles in many diverse biological processes of living organisms ranging from prokaryotes (e.g., Escherichia coli ) to the complex multicellular Homo sapiens (Moutinho et al, 2001; Newton and Smith, 2004; Schaap, 2005; Meier and Gehring, 2006; Lomovatskaya et al, 2008). It has also become clear that plant GCs (e.g., Meier et al, 2010; Qi et al, 2010; Kwezi et al, 2011; Mulaudzi et al, 2011; Irving et al, 2012; Turek and Gehring, 2016) have distinct and varied domain architectures and can be part of multifunctional enzymes or “moonlighting” proteins with two or more distinct functions (Jeffery, 2003; Irving et al, 2012; Muleya et al, 2014; Kwezi et al, 2018; Su et al, 2019). This is likely to be similar in plant ACs, whereby AC domains coexist and cofunction with other domains.…”

Moonlighting Proteins Shine New Light on Molecular Signaling Niches

“…However, over the last decade significant effort has been made to determine if the protein has the capacity to moonlight. These include analyses of protein sequence and structure and functional sites, conserved motifs and domains, protein-protein interaction patterns, assisted with biochemical methods, to decipher protein structure—function relationships, and extensive attempts to create software tools for prediction and annotation of moonlighting proteins and a database of moonlighting proteins have been made [ 18 , 19 , 20 , 21 , 22 ]. Examples of additional catalytic functions are in general less common in the literature [ 3 , 15 ].…”

Discovery of a Nitric Oxide-Responsive Protein in Arabidopsis thaliana

“…Moreover, we have also shown that AtNOGC1 acts as a guanylate cyclase (GC) and that this activity can be modulated in an NO-dependent manner in vitro [13]. It has also been demonstrated that in an AtNOGC1 T-DNA insertion mutant, NO fails to induce stomatal closure, indicating that this “moonlighting” enzyme is central to both NO- and cGMP-dependent stomatal movements, thus establishing the biological relevance of direct NO-sensing [14,15]. It is important to note that AtNOGC1 harbors only the key residues of the H-NOX center that accommodate the heme group and not the full H-NOX domain.…”