Fission yeast Dma1 requires RING domain dimerization for its ubiquitin ligase activity and mitotic checkpoint function.

Johnson AE, Collier SE, Ohi MD, Gould KL
J Biol Chem. 2012 287 (31): 25741-8

PMID: 22669973 · PMCID: PMC3406662 · DOI:10.1074/jbc.M112.349712

In fission yeast (Schizosaccharomyces pombe), the E3 ubiquitin ligase Dma1 delays cytokinesis if chromosomes are not properly attached to the mitotic spindle. Dma1 contains a C-terminal RING domain, and we have found that the Dma1 RING domain forms a stable homodimer. Although the RING domain is required for dimerization, residues in the C-terminal tail are also required to help form or stabilize the dimeric structure because mutation of specific residues in this region disrupts Dma1 dimerization. Further analyses showed that Dma1 dimerization is required for proper localization at spindle pole bodies and the cell division site, E3 ligase activity, and mitotic checkpoint function. Thus, Dma1 forms an obligate dimer via its RING domain, which is essential for efficient transfer of ubiquitin to its substrate(s). This study further supports the mechanistic paradigm that many RING E3 ligases function as RING dimers.

MeSH Terms (15)

Amino Acid Sequence Cell Cycle Proteins Conserved Sequence Mitosis Molecular Sequence Data M Phase Cell Cycle Checkpoints Protein Multimerization Protein Structure, Quaternary Protein Transport RING Finger Domains Schizosaccharomyces Schizosaccharomyces pombe Proteins Sequence Homology, Amino Acid Spindle Apparatus Ubiquitin-Protein Ligases

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