Negatively Charged Lipids Are Essential for Functional and Structural Switch of Human 2-Cys Peroxiredoxin II
In: Journal of Molecular Biology, Jg. 430 (2018-03-01), S. 602-610
Online
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Zugriff:
The function of ubiquitous 2-Cys peroxiredoxins (Prxs) can be converted alternatively from peroxidases to molecular chaperones. This conversion has been reported to occur by the formation of high-molecular-weight (HMW) complexes upon overoxidation of or ATP/ADP binding to 2-Cys Prxs, but its mechanism is not well understood. Here, we show that upon binding to phosphatidylserine or phosphatidylglycerol dimeric human 2-Cys PrxII (hPrxII) is assembled to trefoil-shaped small oligomers (possibly hexamers) with full chaperone and null peroxidase activities. Spherical HMW complexes are formed, only when phosphatidylserine or phosphatidylglycerol is bound to overoxidized or ATP/ADP-bound hPrxII. The spherical HMW complexes are lipid vesicles covered with trefoil-shaped oligomers arranged in a hexagonal lattice pattern. Thus, these lipids with a net negative charge, which can be supplied by increased membrane trafficking under oxidative stress, are essential for the structural and functional switch of hPrxII and possibly most 2-Cys Prxs.
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Negatively Charged Lipids Are Essential for Functional and Structural Switch of Human 2-Cys Peroxiredoxin II
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Autor/in / Beteiligte Person: | Kodera, Noriyuki ; Yamada, Yutaro ; Ando, Toshio ; Haruyama, Takamitsu ; Konno, Hiroki ; Uchihashi, Takayuki |
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Zeitschrift: | Journal of Molecular Biology, Jg. 430 (2018-03-01), S. 602-610 |
Veröffentlichung: | Elsevier BV, 2018 |
Medientyp: | unknown |
ISSN: | 0022-2836 (print) |
DOI: | 10.1016/j.jmb.2017.12.020 |
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