Towards the identification of protein complexes in banana (Musa spp) meristems

• Authors : Vertommen, A.; Carpentier, S.; Remmerie, N.; Witters, E.; Swennen, R.; Panis, B.


• Document type : Journal article


• Year of publication : 2007


• Journal title : Communications in Agricultural and Applied Biological Sciences


• Volume (number) : 72 (1)




• Pages : 4


• Peer-reviewed : Yes


• ISSN : 1379-1176


• Language(s) : English


• Abstract : The preferred method to safely preserve the banana biodiversity is cryopreservation (or storage at -196°C). Successful application of this technique requires sufficient removal of tissue water (dehydration phase), generally preceded by an acclimation phase (Panis et al., 1996). To get more insight into the physiological processes during that acclimation period, it is important to understand which proteins are involved and how they interact with each other. To analyze proteins of poorly sequenced species, like banana (Musa spp.), two dimensional gel electrophoresis (2DE), protein quantification and identification through tandem mass spectrometry (MS/MS) is the method of preference (Carpentier et al., 2005; Samyn et al., 2007; Carpentier et al., 2007). However, classical 2DE is highly denaturating, which results in loss of information about the organization of protein complexes and/or protein-protein interactions. Moreover, hydrophobic proteins are difficult to analyze since they tend to precipitate during first dimension iso-electric focusing. To solve these problems, Schägger and von Jagow (1991) developed Blue native PAGE (BN-PAGE) which allows separation of protein complexes as well as hydrophobic proteins in the mass range of 10 kDa to 1 MDa. This technique comprises (i) the use of mild, neutral detergents for solubilisation and (ii) the application of Coomassie Brilliant Blue G250 to give a negative charge to proteins and protein complexes. This permits separation according to their mass. In plants, protein complexes of organelles have been most intensively investigated. Till now, there are no publications on protein complexes from whole cellular lysates of plants which makes optimizing BNPAGE to study complexes in banana meristems a real challenge. Even more since, we are dealing with limited amounts of tissue of a recalcitrant nonmodel crop.


• Keywords : ELECTROPHORESIS; PROTEINS; IDENTIFICATION; MERISTEMS; ANALYTICAL METHODS


• Open access : No


• Document on publisher's site : View article on publisher's site


• Musalit document ID : IN080326

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