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A mutant of Arabidopsis thaliana partially resistant to fusicoccin has reduced plasma membrane H + ‐ATPase
Author(s) -
MICHELIS M. I.,
PUGLIARELLO M. C.,
RASICALDOGNO F.,
SOAVE C.
Publication year - 1996
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/j.1365-3040.1996.tb00259.x
Subject(s) - fusicoccin , mutant , atpase , wild type , arabidopsis thaliana , biochemistry , microbiology and biotechnology , membrane , blot , biology , chemistry , enzyme , gene
5‐2 is a mutant of Arabidopsis thaliana which is partially resistant to fusicoccin in vivo . We have analysed fusicoccin binding and the activity and amount of H + ‐ATPase in plasma membrane isolated from mature leaves of the wild type and of mutant 5‐2 . Fusicoccin binding was similar in plasma membrane from the two genotypes, while H + ‐ATPase activity was markedly ( c . 50%) lower in plasma membrane from mutant 5‐2 than in that from the wild type. The H + ‐ATPase of mutant 5‐2 was activated by fusicoccin as much as that of the wild type. In plasma membrane from mutant 5‐2 , the amount of immunodetectable H + ‐ATPase, quantified by densitometry of Western blots, was about half that in the wild type. These results indicate that the major defect of mutant 5‐2 detectable at the plasma membrane level is a reduction in the amount of H + ‐ATPase.