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When an Enzyme Isn't Just an Enzyme Anymore Extra Botany

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When an Enzyme Isn't Just an Enzyme Anymore Extra Botany eXtra Botany Insight When an enzyme isn’t just an enzyme anymore Brenda S.J. Winkel Department of Biological Sciences, Virginia Tech, Blacksburg, VA 24060, USA [email protected] In this issue (pages 1425–1440) Bross et al. provide evi- There are numerous other examples of glycolytic enzymes dence of surprising alternative functions for two iso- with alternative non-catalytic functions, though none as inten- forms of the plastid enzyme arogenate dehydratase. sively studied as GAPDH (Jeffery, 2014). The functions of This study points to a previously unsuspected con- these proteins range from serving as transcriptional regulators nection between central metabolism and chloroplast that are sensitive to sucrose concentrations to binding of plas- division and a potential new mechanism for retrograde minogen during microbial pathogenesis (Rolland et al., 2006; signaling. These findings add to a growing awareness He et al., 2013; Henderson and Martin, 2013; Vega et al., of the complexities of protein function that has sub- 2016). Dual functionality is also associated with enzymes of stantial implications for both basic and applied plant many other pathways of central metabolism, such as homoci- science. trate synthase, which is essential for lysine biosynthesis in mitochondria but can also mediate DNA repair in the nucleus We are in the midst of a paradigm shift in our understanding (Torres-Machorro et al., 2015). Aconitase is another well- of cellular metabolism, as growing numbers of proteins with established example, functioning not only as a key enzyme well-established catalytic roles are being found to have addi- in the TCA cycle, but also as an iron-responsive protein that tional, alternative functions. Although the pervasiveness of enhances synthesis of proteins involved in iron uptake under this so-called ‘moonlighting’ phenomenon is not yet clear, the low intracellular iron concentrations, a role conserved from MoonProt database (www.moonlightingproteins.org) already microbes to plants and animals (Commichau and Stulke, 2008; has almost 300 entries for multifunctional proteins from across Marondedze et al., 2016). Multifunctional proteins are also the phylogenetic spectrum, including many originally identi- behind the increasingly apparent connection between central fied as enzymes of central metabolism. The rapid pace with metabolism and chromatin dynamics (Keating and El-Osta, which new and alternative functions are being reported sug- 2015). For example, the mammalian NCOAT enzyme that gests that current knowledge represents the tip of an iceberg. removes GlcN modifications from nuclear and cytoplasmic proteins also functions as a histone acetyltransferase affect- ing chromatin status (Toleman et al., 2004). Similarly, a recent Linking biological processes screen for proteins that function in heterochromatin regula- An emerging theme surrounding moonlighting proteins tion revealed a novel role for glutamate dehydrogenase in telo- is that multi-functionality can provide a powerful mecha- meric silencing (Su and Pillus, 2016). nism to link diverse cellular processes, including across cellular compartments. Glyceraldehyde-3-phosphate dehy- drogenase (GAPDH), a cytoplasmic glycolytic enzyme, is The special case of the plant cell a remarkable example. GAPDH protein has been found to be localized to a wide range of sites in many different The unique architecture of the plant cell, which includes plas- organisms, from microbes to plants and animals (He et al., tids as well as other structures present only in plants, together 2013; Zaffagnini et al., 2013; Sirover, 2014). At these vari- with an unusually complex metabolism, suggests that plant ous sites GAPDH has been found to participate not only in evolution has offered unique opportunities for recruitment glycolysis, but in pathogenesis, receptor-mediated cell sign- of enzymes into novel functions. Indeed, plants are proving aling, iron metabolism, histone biosynthesis, and control of to be invaluable platforms for the discovery and characteriza- cell cycle progression (Frederikse et al., 2016), while also tion of multifunctional proteins, often pointing to novel acces- serving as a redox sensor and transducer. In these ways, sory activities not present in other organisms. For example, in GAPDH is able to integrate multiple biological processes Arabidopsis, the L10 ribosomal protein was found to func- in response to changes in the metabolic and redox status tion not only in protein synthesis in the cytosol, but also to of the cell, a role with an apparently ancient evolutionary contribute to the restriction of virus infection in the nucleus origin (Hildebrandt et al., 2015). in an as-yet-undetermined manner; this is distinct from the © The Author 2017. Published by Oxford University Press on behalf of the Society for Experimental Biology. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. 1388 | moonlighting functions identified for L10 and other ribosomal (Bross et al., 2017). This study adds a new spin to the idea proteins in microbes, yeast, Drosophila, and humans, although of moonlighting, showing for the first time a connection in both plants and humans phosphorylation may be involved between central metabolism and organelle division in plants, in directing L10 to the nucleus (Warner and McIntosh, 2009). specifically components of the chloroplast division machin- Plants have also provided intriguing examples of closely ery. Arogenate dehydratases (ADTs) are found only in plants related genes encoding proteins with a shared catalytic func- and some groups of microbes, where they play an important tion but a diversity of accessory functions, as in the case of the role in phenylalanine biosynthesis. The new study provides an germin and germin-like proteins (Li et al., 2016). These super- in-depth analysis of the localization of the six Arabidopsis oxide dismutases exhibit a wide array of alternative functions, ADT isoforms, all of which are targeted, by virtue of a tran- including as oxalate oxidases, as auxin receptors, and as poly- sit peptide, to the stroma and stromules of chloroplasts. This phenol oxidase and serine protease inhibitors in a variety of extends previous reports on the presence of these six proteins plant species. In another extension of work in other organisms, in chloroplasts, as also reported for four ADTs from Pinus studies in Arabidopsis link inositol metabolism to plant defense pinaster (Rippert et al., 2009; El-Azaz et al., 2016). Bross through histone remodeling (Latrasse et al., 2013). In this case, et al. now show that two of the isoforms have additional myo-inositol phosphate synthase, a cytoplasmic enzyme, inter- localizations that point to non-catalytic functions. Confocal acts with the histone methyltransferases ATXR5 and ATXR6, microscopy of constructs transiently expressed in tobacco in the nucleus, controlling its own expression via histone modi- and Arabidopsis (the latter an important technical innova- fication, including in response to pathogens. Reports of novel tion), together with insights from mutant analysis, suggest localization of components of well-established pathways con- that ADT2 participates in the plastid division process as one tinue to mount in plants, suggesting that there are many more of the as-yet-unidentified components of a plastid division dual functionalities waiting to be uncovered, including among ring. Similar analyses show that another isoform, ADT5, has the enzymes of specialized metabolism (Box 1). an additional location in the nucleus, suggesting the intrigu- ing possibility that it could be involved in retrograde signaling A new dimension to moonlighting from the plastid to influence nuclear gene expression. The isoform-specific differential roles of the plant ADTs One of the latest discoveries is described in the paper from raise the question of how and when such multifunctional enti- Susanne Kohalmi’s group at Western University in Ontario ties might evolve within a group of closely related proteins. Comprehensive phylogenetic analyses previously classified the plant ADTs into four subgroups that are distinct from the groups encompassing microbial ADTs, including those in the Box 1. The potential for moonlighting Bacterioidetes/Chlorobi, which represent the closest bacterial The flavonoid enzyme, chalcone isomerase, localizes to homologs (Dornfeld et al., 2014; El-Azaz et al., 2016). This both the ER and the nucleus in Arabidopsis root cells. analysis further suggests that plant ADTs diversified following Fixed whole-mount seedlings were labeled with antibod- the split of plants and chlorophytes (green algae), with present- ies specific for CHI (red) and the ER-resident protein BiP day ADTs having evolved from the subfamily I-type enzymes (green), nuclei were counterstained with DAPI (blue), and to which ADT2 belongs. This phylogeny further indicates that samples were optically sectioned by confocal micros- ADT2 is more closely related to ADT enzymes in other plants copy as described in Saslowsky et al., 2005. Image by than its homologs in Arabidopsis, suggesting that its role in David E. Saslowsky. plastid division predates an early split in the green lineage. This phylogeny also indicates that ADT4 and ADT5 are closely related, offering the possibility for defining sequences involved
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