Laukens K, Roef L, Witters E, Slegers H, Van Onckelen H
Laboratorium voor Plantenbiochemie en -fysiologie, Department of Biology, University of Antwerp (UIA), Universiteitsplein 1, B-2610 Antwerp, Belgium.
FEBS Lett. 2001 Nov 9;508(1):75-9. doi: 10.1016/s0014-5793(01)03026-5.
The soluble protein fraction of tobacco bright yellow 2 cells contained adenosine 3',5'-cyclic monophosphate (cAMP)-binding activity, detected with both a conventional binding assay and a surface plasmon resonance biosensor. A cAMP-agarose-based affinity purification procedure yielded three proteins which were identified by mass spectrometry as glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and two nucleoside diphosphate kinases (NDPKs). This is the first report describing an interaction between cAMP and these proteins in higher plants. Our findings are discussed in view of the reported role of the interaction of cAMP with GAPDH and NDPK in animals and yeast. In addition, we provide a rapid method to isolate both proteins from higher plants.
