NDLI: Role of strategic cysteine residues in oxidative damage to the yeast plasma membrane H$^{+}$-ATPase caused by Fe- and Cu-containing fenton reagents

Content Provider	Springer Nature Link
Author	Stadler, N. Váchová, L. Krasowska, A. Höfer, M. Sigler, K.
Copyright Year	2003
Abstract	Damage caused toSaccharomyces cerevisiae SY4 plasma membrane H$^{+}$-ATPase by Fe- and Cu-Fenton reagents was determined in secretory vesicles containing enzyme in which Cys residues were replaced singly or in pairs by Ala. Cys-221 situated in a β-sheet domain between M2 and M3 segments, phosphorylation domain-located Cys-409 and Cys-532 situated at the ATP-binding site play a role in the inactivation. In the presence of all three residues the enzyme exhibited a certain basic inactivation, which did not change when Cys-532 was replaced with Ala. In mutants having intact Cys-532 but lacking one or both other cysteines, replacement of Cys-221 with Ala led to lower inactivation, suggesting that Cys-221 may serve as a target for metal-catalyzed oxidation and intact Cys-532 promotes this target role of Cys-221. In contrast, the absence of Cys-409 caused higher inactivation by Fe-Fenton. Cys-532 thus seems to serve as a target for Fe-Fenton, intact Cys-409 causing a conformational change that makes Cys-532 less accessible to oxidation. The mutant lacking both Cys-221 and Cys-409 is more sensitive to Fe-Fenton than to Cu-Fenton and the absence of both Cys residues thus seems to expose presumable extra Fe-binding sites. These data and those on protection by ATP, ADP, 1,4-dithiothreitol and deferrioxamine B point to complex interactions between individual parts of the enzyme molecule that determine its sensitivity towards Fenton reagents. ATPase fragmentation caused by the two reagents differed in that the Fe-Fenton reagent produced in Western blot “smears” whereas the Cu-Fenton reagent produced defined fragments.
Starting Page	589
Ending Page	596
Page Count	8
File Format	PDF
ISSN	00155632
Journal	Folia Microbiologica
Volume Number	48
Issue Number	5
e-ISSN	18749356
Language	English
Publisher	Springer Netherlands
Publisher Date	2003-01-01
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Life Sciences Microbiology Applied Microbiology Immunology Environmental Engineering/Biotechnology
Content Type	Text
Resource Type	Article
Subject	Medicine Microbiology

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