Dissection of the Dimerization Modes in the DJ-1 Superfamily
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Title
- Dissection of the Dimerization Modes in the DJ-1 Superfamily
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Author(s)
- Jung, Hoi Jong; Kim, Sangok; Kim, Yun Jae; Kim, Min-Kyu; Kang, Sung Gyun; Lee, Jung-Hyun; Kim, Wankyu; Cha, Sun-Shin
- KIOST Author(s)
- Kim, Yun Jae(김윤재); Kang, Sung Gyun(강성균); Lee, Jung Hyun(이정현)
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Alternative Author(s)
- 정회종; 김윤재; 김민규; 강성균; 이정현; 차선신
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Publication Year
- 2012-02
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Abstract
- 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.
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ISSN
- 1016-8478
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/3631
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DOI
- 10.1007/s10059-012-2220-6
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Bibliographic Citation
- MOLECULES AND CELLS, v.33, no.2, pp.163 - 171, 2012
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Publisher
- KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
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Subject
- RESOLUTION CRYSTAL-STRUCTURE; ESCHERICHIA-COLI HSP31; DISEASE PROTEIN DJ-1; SACCHAROMYCES-CEREVISIAE; INTRACELLULAR PROTEASE; OXIDATIVE STRESS; MEMBER; GENE; EVOLUTIONARY; DOMAIN
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Keywords
- DJ-1 superfamily; DJ-1/ThiJ/PfpI superfamily; quaternary structure
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Type
- Article
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Language
- English
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Document Type
- Article
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