Dissection of the Dimerization Modes in the DJ-1 Superfamily

• Published in: Molecules and cells Vol. 33; no. 2; pp. 163 - 171
• Main Authors: Jung, H.J., Marine Biotechnology Research Center, Korea Ocean Research and Development Institute, Ansan, Republic of Korea, Kim, S.O., Ewha Womans University, Seoul, Republic of Korea, Kim, Y.J., Marine Biotechnology Research Center, Korea Ocean Research and Development Institute, Ansan, Republic of Korea, Kim, M.K., Marine Biotechnology Research Center, Korea Ocean Research and Development Institute, Ansan, Republic of Korea, Kang, S.G., Marine Biotechnology Research Center, Korea Ocean Research and Development Institute, Ansan, Republic of Korea, Lee, J.H., Marine Biotechnology Research Center, Korea Ocean Research and Development Institute, Ansan, Republic of Korea, Kim, W.K., Ewha Womans University, Seoul, Republic of Korea, Cha, S.S., Marine Biotechnology Research Center, Korea Ocean Research and Development Institute, Ansan, Republic of Korea
• Format: Journal Article
• Language: English
• Published: Springer Korean Society for Molecular and Cellular Biology 01-02-2012; Korea Society for Molecular and Cellular Biology; 한국분자세포생물학회
• Subjects: Binding Sites - genetics; Biochemistry; Biomedical and Life Sciences; Biomedicine; Biotechnology; Cell Biology; Computational Biology; Crystallography, X-Ray; DJ-1 superfamily; Evolution, Molecular; Humans; Intracellular Signaling Peptides and Proteins - chemistry; Intracellular Signaling Peptides and Proteins - classification; Intracellular Signaling Peptides and Proteins - genetics; Life Sciences; Molecular Chaperones - chemistry; Molecular Chaperones - classification; Molecular Chaperones - genetics; Mutation Rate; Oncogene Proteins - chemistry; Oncogene Proteins - classification; Oncogene Proteins - genetics; Parkinson Disease - genetics; Parkinson Disease - metabolism; Phylogeny; Protein Binding - genetics; Protein Deglycase DJ-1; Protein Multimerization; Protein Structure, Quaternary; PROTEINAS; PROTEINE; PROTEINS; quaternary structure; Structure-Activity Relationship; 생물학; quaternary structure; DJ-1 superfamily; DJ-1/ThiJ/PfpI superfamily
• ISSN: 1016-8478; 0219-1032
• DOI: 10.1007/s10059-012-2220-6

The DJ-1 superfamily (DJ-1/ThiJ/PfpI superfamily) is distributed across all three kingdoms of life. These proteins are involved in a highly diverse range of cellular functions, including chaperone and protease activity. DJ-1 proteins usually form dimers or hexamers in vivo and show at least four different binding orientations via distinct interface patches. Abnormal oligomerization of human DJ-1 is related to neurodegenerative disorders including Parkinson's disease, suggesting important functional roles of quaternary structures. However, the quaternary structures of the DJ-1 superfamily have not been extensively studied. Here, we focus on the diverse oligomerization modes among the DJ-1 superfamily proteins and investigate the functional roles of quaternary structures both computationally and experimentally. The oligomerization modes are classified into 4 types (DJ-1, YhbO, Hsp, and YDR types) depending on the distinct interface patches (Ⅰ-Ⅳ) upon dimerization. A unique, rotated interface via patch I is reported, which may potentially be related to higher order oligomerization. In general, the groups based on sequence similarity are consistent with the quaternary structural classes, but their biochemical functions cannot be directly inferred using sequence information alone. The observed phyletic pattern suggests the dynamic nature of quaternary structures in the course of evolution. The amino acid residues at the interfaces tend to show lower mutation rates than those of non-interfacial surfaces.