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First evidence and characterization of an uncoupling protein in fungi kingdom: CpUCP of Candida parapsilosis
Author(s) -
Jarmuszkiewicz Wiesława,
Milani Graziela,
Fortes Fabiane,
Schreiber Angelica Z.,
Sluse Francis E.,
Vercesi Anibal E.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01138-8
Subject(s) - candida parapsilosis , uncoupling protein , oxidative phosphorylation , yeast , mitochondrion , biology , biochemistry , gtp' , alternative oxidase , polyclonal antibodies , botany , enzyme , antibody , candida albicans , adipose tissue , immunology , brown adipose tissue
An uncoupling protein (UCP) was identified in mitochondria from Candida parapsilosis (CpUCP), a non‐fermentative parasitic yeast. CpUCP was immunodetected using polyclonal antibodies raised against plant UCP. Activity of CpUCP, investigated in mitochondria depleted of free fatty acids, was stimulated by linoleic acid (LA) and inhibited by GTP. Activity of CpUCP enhanced state 4 respiration by decreasing Δ Ψ and lowered the ADP/O ratio. Thus, it was able to divert energy from oxidative phosphorylation. The voltage dependence of electron flux indicated that LA had a pure protonophoretic effect. The discovery of CpUCP proves that UCP‐like proteins occur in the four eukaryotic kingdoms: animals, plants, fungi and protists.

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