Plant and Cell Physiology Advance Access originally published online on April 19, 2005
Plant and Cell Physiology 2005 46(6):997-1006; doi:10.1093/pcp/pci108
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NADP-malic Enzyme and Hsp70: Co-purification of Both Proteins and Modification of NADP-malic Enzyme Properties by Association with Hsp70
1 Centro de Estudios Fotosintéticos y Bioquímicos, Facultad de Ciencias Bioquímicas y Farmacéuticas, Suipacha 531, Rosario (2000), Argentina
2 Botanisches Institut, Universität zu Köln, Gyrhofstr. 15, D-50931, Cologne, Germany
3 Corresponding author: E-mail, candreo{at}fbioyf.unr.edu.ar; Fax, +54-341-4370044.
Different preparations of antibodies against 62 kDa NADP-malic enzyme (NADP-ME) from purified maize leaves cross-react with a 72 kDa protein from diverse tissues in many species. A 72 kDa protein, suggested to be a non-photosynthetic NADP-ME, has been purified from several plant species. However, to date, a cDNA coding for this putative 72 kDa NADP-ME has not been isolated. The screening of maize and tobacco leaf expression libraries using antibodies against purified 62 kDa NADP-ME allowed the identification of a heat shock protein (Hsp70). In addition, tandem mass spectrometry (MS/MS) studies indicate that along with NADP-ME, a 72 kDa protein, identified as an Hsp70 and reacting with the antibodies, is also purified from maize roots. On the other hand, the screening of a maize root cDNA library revealed the existence of a cDNA that encodes a mature 66 kDa NADP-ME. These results suggest that the 72 kDa protein is not actually an NADP-ME but in fact an Hsp70, at least in maize and tobacco. Probably, NADP-ME–Hsp70 association, taking place at least when preparing crude extracts, can lead to a co-purification of the proteins and can thus explain the cross-reaction of the antibodies. In the present work, we analyse and discuss a probable interaction of NADP-ME with Hsp70.
(Received February 9, 2005; Accepted April 9, 2005)
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