Identification of a Bromodomain-like region in 15-Lipoxygenase-1 explains its Nuclear Localization

Deng Chen, Zhangping Xiao, Hao Guo, Dea Gogishvili, Rita Setroikromo, Petra E van der Wouden, Frank J Dekker*

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

2 Citaten (Scopus)
24 Downloads (Pure)

Samenvatting

Lipoxygenase (LOX) activity provides oxidative lipid metabolites, which are involved in inflammatory disorders and tumorigenesis. Activity-based probes to detect the activity of LOX enzymes in their cellular context provide opportunities to explore LOX biology and LOX inhibition. Here, we developed Labelox B as a potent covalent LOX inhibitor for one-step activity-based labelling of proteins with LOXs activity. Labelox B was used to establish an ELISA-based assay for affinity capture and antibody-based detection of specific LOX isoenzymes. Moreover, Labelox B enabled efficient activity-based labeling of endogenous LOXs in living cells. LOX proved to localize in the nucleus, which was rationalized by identification of a functional bromodomain-like consensus motif in 15-LOX-1. This indicates that 15-LOX-1 is not only involved in oxidative lipid metabolism, but also in chromatin binding, which suggests a potential role in chromatin modifications.

Originele taal-2English
Pagina's (van-tot)21875-21883
Aantal pagina's21875
TijdschriftAngewandte Chemie (International ed. in English)
Volume60
Nummer van het tijdschrift40
Vroegere onlinedatum13-aug.-2021
DOI's
StatusPublished - 27-sep.-2021

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