View : 2 Download: 0
Structural basis for the interaction between DJ-1 and Bcl-XL
- Structural basis for the interaction between DJ-1 and Bcl-XL
- Lee M.-K.; Lee M.-S.; Bae D.-W.; Lee D.-H.; Cha S.-S.; Chi S.-W.
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- Biochemical and Biophysical Research Communications
- vol. 495, no. 1, pp. 1067 - 1073
- Bcl-XL; Complex structure; DJ-1; NMR spectroscopy; Protein interaction
- Elsevier B.V.
- SCI; SCIE; SCOPUS
- DJ-1 is a multifunctional protein associated with Parkinson's disease (PD) and tumorigenesis. In response to ultraviolet B (UVB) irradiation, DJ-1 is translocated into the mitochondria, and its interaction with the mitochondrial protein Bcl-XL protects cells against death. In this study, we characterized the molecular interaction between DJ-1 and Bcl-XL by NMR spectroscopy. The NMR chemical shift perturbation data demonstrated that the oxidized but not the reduced form of DJ-1 binds to the predominantly hydrophobic groove surrounded by the BH1–BH3 domains in Bcl-XL. In addition, our results showed that the C-terminal α8-helix peptide (Cpep) of DJ-1 binds to the pro-apoptotic BH3 peptide-binding hydrophobic groove in Bcl-XL and, thus, acts as a Bcl-XL-binding motif. In combination with the NMR chemical shift perturbation data, a refined structural model of the Bcl-XL/DJ-1 Cpep complex revealed that the binding mode is remarkably similar to that of other Bcl-XL/pro-apoptotic BH3 peptide complexes. Taken together, our results provide a structural basis for the binding mechanism between DJ-1 and Bcl-XL, which will contribute to molecular understanding of the role of mitochondrial DJ-1 in Bcl-XL regulation in response to oxidative stress. © 2017 Elsevier Inc.
- Appears in Collections:
- 자연과학대학 > 화학·나노과학전공 > Journal papers
- Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.