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Dissection of the dimerization modes in the DJ-1 superfamily

Title
Dissection of the dimerization modes in the DJ-1 superfamily
Authors
Jung H.J.Kim S.Kim Y.J.Kim M.-K.Kang S.G.Lee J.-H.Kim W.Cha S.-S.
Ewha Authors
김완규
SCOPUS Author ID
김완규scopus
Issue Date
2012
Journal Title
Molecules and Cells
ISSN
1016-8478JCR Link
Citation
vol. 33, no. 2, pp. 163 - 171
Indexed
SCI; SCIE; SCOPUS; KCI WOS scopus
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. © 2012 KSMCB.
DOI
10.1007/s10059-012-2220-6
Appears in Collections:
자연과학대학 > 생명과학전공 > Journal papers
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