Plant and Cell Physiology Advance Access published online on April 22, 2007
Plant and Cell Physiology, doi:10.1093/pcp/pcm047
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Regulatory properties of potato-Arabidopsis hybrid ADP-Glucose Pyrophosphorylase
1 Instituto de Bioquímica Vegetal y Fotosíntesis, Centro de Investigaciones Científicas Isla de la Cartuja, Universidad de Sevilla-C.S.I.C., c/ Americo Vespucio N° 49, 41092-Sevilla, Spain
2 Department of Biochemistry, Michigan State University, East Lansing, Michigan 48824.
3 Present address: Dept. of Chemistry, Loyola University Chicago. 405 Flanner Hall, 1068 W. Sheridan Rd. Chicago, IL 60626.
4 Present Address: Department of Cell and Development Biology, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, U.K.
*Corresponding author: José M. Romero. Instituto de Bioquímica Vegetal y Fotosíntesis, Centro de Investigaciones Científicas Isla de la Cartuja, Universidad de Sevilla-C.S.I.C., c/ Americo Vespucio N° 49, 41092-Sevilla, Spain. Telf: +34-954489526, FAX: + 34-954460065, E-mail: jmromero{at}ibvf.csic.es
| Abstract |
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In higher plants, ADP-glucose pyrophosphorylase (ADPGlc-PPase) is a heterotetrameric enzyme comprised by two small and two large subunits. Potato/Arabidopsis hybrid ADPGlc-PPases were generated and their regulatory properties analyzed. We show that ADPGlc-PPase subunits from two different species can interact rendering active enzymes with new regulatory properties. Depending on subunit combinations, hybrid heterotetramers showed responses to the allosteric effectors (3-PGA and Pi) in the µM or mM range. While hybrid potato small subunit (PSS) and the Arabidopsis large subunit APL1 showed an extremely sensitive response to 3-PGA and Pi, hybrid PSS/Arabidopsis APL2 was very insensitive to them. Intermediate responses were determined for other subunit combinations.
Keywords: ADP-glucose pyrophosphorylase - allosteric regulation - Arabidopsis thaliana - heterotetrameric enzyme - hybrid-enzyme - potato
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