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Differential Immunological Cross-Reactions with Antisera against the V-ATPase of Kalanchoë daigremontiana Reveal Structural Differences of V-ATPase Subunits of Different Plant Species

Fischer-Schliebs, Elke ; Ball, Erika ; Berndt, Ekkehart ; Besemfelder-Butz, Eva ; Binzel, Marla L. ; Drobny, Martina ; Mühlenhoff, Dagmar ; Müller, Mathias L. ; Rakowski, Krzysztof ; Ratajczak, Rafael (1997)
Differential Immunological Cross-Reactions with Antisera against the V-ATPase of Kalanchoë daigremontiana Reveal Structural Differences of V-ATPase Subunits of Different Plant Species.
In: Biological chemistry, 378 (10)
doi: 10.1515/bchm.1997.378.10.1131
Article, Bibliographie

Abstract

Two antisera (ATP88 and ATP95) raised against the V-ATPase holoenzyme of Kalanchoe daigremontianawere tested for their cross-reactivity with subunits ofV-ATPases from other plant species. V-ATPases fromKalanchoe blossfeldiana, Mesembryanthemum crys-tallinum, Nicotians tabacum, Lycopersicon esculentum, Citrus limon, Lemna gibba, Hordeum vulgäre and Zea mays were immunoprecipitated with an antiserumagainst the catalytic V-ATPase subunit A of M. crystal-linum. As shown by silver staining and Western blotanalysis with ATP88, subunits A, B, C, D and c werepresent in all immunoprecipitated V-ATPases. In contrast, ATP95 recognized the whole set of subunits onlyin K. blossfeldiana, M. crystallinum, H. vulgäre and Z.mays. This differential cross reactivity of ATP95 indicates the presence of structural differences of certainV-ATPase subunits. Based on the Bafilomycin A1-sen-sitive ATPase activity of tonoplast enriched vesicles, and on the amount of V-ATPase solubilized and immunoprecipitated, the specific ATP-hydrolysis activity ofthe V-ATPases under test was determined. The structural differences correlate with the ability of V-ATPases from different species to hydrolyze ATP atone given assay condition for ATP-hydrolysis measu-rements. Interestingly V-ATPases showing crossreactivity of subunits A, B, C, D and c with ATP95 showedhigher rates of specific ATP hydrolysis compared to V-ATPases containing subunits which were not labeledby 95. Thus, V-ATPases with high turnover rates in our assay conditions may show common structuralcharacteristics which separate them from ATPases with low turnover rates.

Item Type: Article
Erschienen: 1997
Creators: Fischer-Schliebs, Elke ; Ball, Erika ; Berndt, Ekkehart ; Besemfelder-Butz, Eva ; Binzel, Marla L. ; Drobny, Martina ; Mühlenhoff, Dagmar ; Müller, Mathias L. ; Rakowski, Krzysztof ; Ratajczak, Rafael
Type of entry: Bibliographie
Title: Differential Immunological Cross-Reactions with Antisera against the V-ATPase of Kalanchoë daigremontiana Reveal Structural Differences of V-ATPase Subunits of Different Plant Species
Language: English
Date: 1 October 1997
Publisher: De Gruyter
Journal or Publication Title: Biological chemistry
Volume of the journal: 378
Issue Number: 10
DOI: 10.1515/bchm.1997.378.10.1131
Abstract:

Two antisera (ATP88 and ATP95) raised against the V-ATPase holoenzyme of Kalanchoe daigremontianawere tested for their cross-reactivity with subunits ofV-ATPases from other plant species. V-ATPases fromKalanchoe blossfeldiana, Mesembryanthemum crys-tallinum, Nicotians tabacum, Lycopersicon esculentum, Citrus limon, Lemna gibba, Hordeum vulgäre and Zea mays were immunoprecipitated with an antiserumagainst the catalytic V-ATPase subunit A of M. crystal-linum. As shown by silver staining and Western blotanalysis with ATP88, subunits A, B, C, D and c werepresent in all immunoprecipitated V-ATPases. In contrast, ATP95 recognized the whole set of subunits onlyin K. blossfeldiana, M. crystallinum, H. vulgäre and Z.mays. This differential cross reactivity of ATP95 indicates the presence of structural differences of certainV-ATPase subunits. Based on the Bafilomycin A1-sen-sitive ATPase activity of tonoplast enriched vesicles, and on the amount of V-ATPase solubilized and immunoprecipitated, the specific ATP-hydrolysis activity ofthe V-ATPases under test was determined. The structural differences correlate with the ability of V-ATPases from different species to hydrolyze ATP atone given assay condition for ATP-hydrolysis measu-rements. Interestingly V-ATPases showing crossreactivity of subunits A, B, C, D and c with ATP95 showedhigher rates of specific ATP hydrolysis compared to V-ATPases containing subunits which were not labeledby 95. Thus, V-ATPases with high turnover rates in our assay conditions may show common structuralcharacteristics which separate them from ATPases with low turnover rates.

Divisions: 10 Department of Biology
10 Department of Biology > Botanischer Garten
Date Deposited: 19 Nov 2008 16:02
Last Modified: 11 Aug 2023 14:25
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