期刊
MOLECULES AND CELLS
卷 33, 期 2, 页码 163-171出版社
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
DOI: 10.1007/s10059-012-2220-6
关键词
DJ-1 superfamily; DJ-1/ThiJ/PfpI superfamily; quaternary structure
资金
- Marine and Extreme Genome Research Center of the Ministry of Land, Transport and Maritime Affairs
- KORDI [PE98513]
- Ministry of Land, Transport and Maritime Affairs
- National Research Foundation of Korea [2009-0084757]
- Ewha Womans University
- Global Frontier Project grant [NRF-M1AXA-002-2010-0029763]
- National Research Foundation [2011-0014992]
- Ministry of Education, Science and Technology of Korea
- National Research Foundation of Korea [2009-0084757, 2011-0014992] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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