The Arabidopsis thaliana ortholog of a purported maize cholinesterase gene encodes a GDSL-lipase
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The Arabidopsis thaliana ortholog of a purported maize cholinesterase gene encodes a GDSL-lipase Mrinalini Muralidharan • Kristina Buss • Katherine E. Larrimore • Nicholas A. Segerson Latha Kannan • Tsafrir S. Mor
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Received: 30 August 2012 / Accepted: 1 February 2013 / Published online: 22 February 2013 Ó Springer Science+Business Media Dordrecht 2013
Abstract Acetylcholinesterase is an enzyme that is intimately associated with regulation of synaptic transmission in the cholinergic nervous system and in neuromuscular junctions of animals. However the presence of cholinesterase activity has been described also in non-metazoan organisms such as slime molds, fungi and plants. More recently, a gene purportedly encoding for acetylcholinesterase was cloned from maize. We have cloned the Arabidopsis thaliana homolog of the Zea mays gene, At3g26430, and studied its biochemical properties. Our results indicate that the protein encoded by the gene exhibited lipase activity with preference to long chain substrates but did not hydrolyze choline esters. The At3g26430 protein belongs to the SGNH clan of serine hydrolases, and more specifically to the GDS(L) lipase family. Keywords Cholinesterase GDS(L)lipase Serine hydrolase
Introduction The evolutionary history of acetylcholine (ACh) as a neurotransmitter can be traced as far back as primitive
Electronic supplementary material The online version of this article (doi:10.1007/s11103-013-0021-8) contains supplementary material, which is available to authorized users. M. Muralidharan K. Buss K. E. Larrimore N. A. Segerson L. Kannan T. S. Mor (&) School of Life Sciences and The Biodesign Institute, Arizona State University, P.O. Box 874501, Tempe, AZ 85287-4501, USA e-mail: [email protected] K. Buss e-mail: [email protected]
bilaterians (e.g. flatworms), but the recruitment of this signaling molecule for other, non-neuronal, functions predates the evolution of the bilaterian lineage (Le Novere and Changeux 1995; Walker et al. 1996; Dent 2006). ACh and enzymes associated with its metabolism have been found not only in cnidrians that lack cholinergic neurons (Denker et al. 2008) and in organisms that altogether lack an organized nervous system (e.g. sponges, Horiuchi et al. 2003) but also in organisms outside of the fungi/metazoan group such as slime molds (Earle and Barclay 1986), ciliates (Delmonte Corrado et al. 2001), algae (Raineri and Modenesi 1986; Gupta et al. 1998), archaea (Yamada et al. 2005) and bacteria (Domenech et al. 1991). In fact, it seems that ACh metabolism is ubiquitous (reviewed in Horiuchi et al. 2003; Kawashima et al. 2007; Wessler and Kirkpatrick 2008). Extensive literature describes the involvement of ACh in several processes in plants (reviewed by Hartmann and Gupta 1989; Tretyn and Kendrick 1991; Wessler et al. 1999; Roshchina 2001). Others and we demonstrated the presence of ACh hydrolytic activity in many plants, and especially in the families Leguminosae and Solanaceae (Fluck and Jaffe 1974; Gupta and Gupta 1997; Fletcher et al.
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