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Photoaffinity labeling of the uncoupling protein UCP1 with retinoic acid: ubiquinone favors binding
Author(s) -
Tomás Paula,
Ledesma Amalia,
Rial Eduardo
Publication year - 2002
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(02)03116-2
Subject(s) - retinoic acid , uncoupling protein , thermogenin , chemistry , biochemistry , brown adipose tissue , adipose tissue , gene
Retinoic acid is a potent activator of the uncoupling protein‐1 (UCP1) both at the gene and mitochondrial level. Irradiation with ultraviolet light can be used to directly photolabel proteins with retinoic acid. The procedure has been applied to investigate its interaction with UCP1 isolated from brown adipose tissue mitochondria. All‐ trans ‐retinoic acid binds to UCP1 with high affinity and the labeling is only partially protected by guanosine diphosphate. Ubiquinone (UQ) has been described to be an obligatory cofactor for uncoupling protein function and we demonstrate that it greatly increases the affinity of UCP1 for retinoic acid. Data support the notion of a direct interaction between UQ and retinoic acid.