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A novel mode of ubiquitin recognition by the ubiquitin‐binding zinc finger domain of WRNIP 1
Author(s) -
Suzuki Nobuhiro,
Rohaim Ahmed,
Kato Ryuichi,
Dikic Ivan,
Wakatsuki Soichi,
Kawasaki Masato
Publication year - 2016
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13734
Subject(s) - zinc finger , ubiquitin , ubiquitin conjugating enzyme , helicase , ring finger domain , fusion protein , ubiquitin ligase , lim domain , microbiology and biotechnology , chemistry , biology , biochemistry , biophysics , transcription factor , gene , recombinant dna , rna
The ubiquitin‐binding zinc finger ( UBZ ) is a type of zinc‐coordinating β‐β‐α fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. Here, we report the crystal structure of the UBZ domain of Y‐family DNA polymerase (pol) η and the crystal structure of the complex between the UBZ domain of Werner helicase‐interacting protein 1 (WRNIP1) and ubiquitin, crystallized using the GFP fusion technique. In contrast to the pol η UBZ , which has been proposed to bind ubiquitin via its C‐terminal α‐helix, ubiquitin binds to a novel surface of WRNIP 1 UBZ composed of the first β‐strand and the C‐terminal α‐helix. In addition, we report the structure of the tandem UBZ domains of Tax1‐binding protein 1 ( TAX 1 BP 1) and show that the second UBZ of TAX 1 BP 1 binds ubiquitin, presumably in a manner similar to that of WRNIP 1 UBZ . We propose that UBZ domains can be divided into at least two different types in terms of the ubiquitin‐binding surfaces: the pol η type and the WRNIP 1 type. Database Structural data are available in the Protein Data Bank under accession numbers 3WUP (pol η UBZ), 3VHS (WRNIP1 UBZ), 3VHT (GFP‐WRNIP1/ubiquitin), 4Z4K (TAX1BP1 UBZ1 + 2), and 4Z4M (TAX1BP1 UBZ2).