AL-INDUCED, 51-KILODALTON, MEMBRANE-BOUND PROTEINS ARE ASSOCIATED WITH RESISTANCE TO AL IN A SEGREGATING POPULATION OF WHEAT

Citation
Gj. Taylor et al., AL-INDUCED, 51-KILODALTON, MEMBRANE-BOUND PROTEINS ARE ASSOCIATED WITH RESISTANCE TO AL IN A SEGREGATING POPULATION OF WHEAT, Plant physiology, 114(1), 1997, pp. 363-372
Citations number
50
Categorie Soggetti
Plant Sciences
Journal title
ISSN journal
00320889
Volume
114
Issue
1
Year of publication
1997
Pages
363 - 372
Database
ISI
SICI code
0032-0889(1997)114:1<363:A5MPAA>2.0.ZU;2-F
Abstract
Incorporation of S-35 into protein is reduced by exposure to Al in whe at (Triticum aestivum), but the effects are genotype-specific. Exposur e to 10 to 75 mu M Al had little effect on S-35 incorporation into tot al protein, nuclear and mitochondrial protein, microsomal protein, and cytosolic protein in the Al-resistant cultivar PT741. In contrast, 10 mu M Al reduced incorporation by 21 to 38% in the Al-sensitive cultiv ar Katepwa, with effects becoming more pronounced (31-62%) as concentr ations of Al increased. We previously reported that a pair of 51-kD me mbrane-hound proteins accumulated in root tips of PT741 under conditio ns of Al stress. We now report that the 51-kD band is labeled with S-3 5 after 24 h of exposure to 75 mu M Al. The specific induction of the 51-kD band in PT741 suggested a potential role of one or both of these proteins in mediating resistance to Al. Therefore, we analyzed their expression in single plants from an F-2, population arising from a cro ss between the PT741 and Katepwa cultivars. Accumulation of 1,3-beta-g lucans (callose) in root tips after 24 h of exposure to 100 mu M Al in dicated that this population segregated for Al resistance in about a 3 :1 ratio. A close correlation between resistance to Al (low callose co ntent of root tips) and accumulation of the 51-kD band was observed, i ndicating that at least one of these proteins cosegregates with the Al -resistance phenotype. As a first step in identifying a possible funct ion, we have demonstrated that the 51-kD band is most clearly associat ed with the tonoplast. Whereas Al has been reported to stimulate the a ctivity of the tonoplast HC-ATPase and H+-PPase, antibodies raised aga inst these proteins did not cross-react with the 51-kD band. Efforts a re now under way to purify this protein from tonoplast-enriched fracti ons.