here - First Legume Society Conference (LSC1)

Book of Abstracts First Legume Society Conference 2013: A Legume Odyssey Novi Sad, Serbia, 9-11 May 2013
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Molecular cloning and characterization of LlACO gene from Lupinus luteus
Emilia Wilmowicz 1 , Agata Kućko 1 , Kamil Frankowski 1 , Jacek Kęsy 1 , Katarzyna Marciniak 1 ,
Paulina Glazińska 1 , Mariusz Banach 1 , Waldemar Wojciechowski 1 , Jan Kopcewicz 1 , Andrzej
Tretyn 2
1 Chair of Plant Physiology and Biotechnology, Nicolaus Copernicus University, Toruń, Poland
2 Centre for modern interdisciplinary technologies, Nicolaus Copernicus University, Toruń, Poland
ACO encodes for 1-aminocyclopropane-1-carboxylate oxidase, the enzyme that catalyzes the
final step of ethylene biosynthesis: oxygen-dependent conversion of 1-aminocyclopropane-1carboxylic
acid (ACC) to ethylene (ET). ACO belongs to a family of mononuclear enzymes that
are characterized by a 2-histidine-1-carboxylic acid iron-binding motif. In this work, we isolated
for the first time cDNA of ACO from leaves of Lupinus luteus (LlACO) and determined its
sequence. The complete coding sequence consists of 951 bp and encodes for 317 amino acids.
Comparison between the deduced amino acid sequence of LlACO and ACO from other plant
species revealed that the predicted sequence contains all of characteristic motifs found in ACOs,
which are essential for their activity: conservative non-heme dioxygenase DIOX_N region, and a
C-terminally located 2OG-FeII_Oxy region. The LlACO gene encodes for a protein which is
similar to that of ACC oxidases identified in other plant species. Our results indicate that
identified cDNA of LlACO encodes most likely an active protein.
Acknowledgements
This research was supported by Ministry of Agriculture and Rural Development grant no 149/2011.
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