Dissection of the dimerization modes in the DJ-1 superfamily

Hoi Jong Jung, Sangok Kim, Yun Jae Kim, Min Kyu Kim, Sung Gyun Kang, Jung Hyun Lee, Wankyu Kim, Sun Shin Cha

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

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.

Original languageEnglish
Pages (from-to)163-171
Number of pages9
JournalMolecules and Cells
Volume33
Issue number2
DOIs
StatePublished - Feb 2012

Keywords

  • DJ-1 superfamily
  • DJ-1/ThiJ/PfpI superfamily
  • Quaternary structure

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