A novel mode of ubiquitin recognition by the ubiquitin‐binding zinc finger domain of WRNIP1. (28th April 2016)

• Record Type: Journal Article
• Authors: Suzuki, Nobuhiro; Rohaim, Ahmed; Kato, Ryuichi; Dikic, Ivan; Wakatsuki, Soichi; Kawasaki, Masato
• Is Part Of: FEBS journal. Volume 283:Number 11(2016)
• Page Start: 2004
• Page End: 2017
• Publication Date: 2016-04-28
• Subjects: green fluorescent protein -- pol η -- TAX1BP1 -- ubiquitin‐binding zinc finger -- WRNIP1; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pathology, Molecular -- Periodicals; 572
• DOI: 10.1111/febs.13734
• Languages: English
• ISSNs: 1742-464X

Abstract

Abstract : 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 WRNIP1 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 (TAX1BP1) and show that the second UBZ of TAX1BP1 binds ubiquitin, presumably in a manner similar to that of WRNIP1 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 WRNIP1 type. Database: Structural data are available in the Protein Data Bank under accession numbers3WUP (pol η UBZ), 3VHS (WRNIP1 UBZ), 3VHT (GFP‐WRNIP1/ubiquitin), 4Z4K (TAX1BP1 UBZ1 + 2), and4Z4M (TAX1BP1 UBZ2). Abstract : Ubiquitin‐binding zinc fingers (UBZs) are small domains found chiefly in proteins involved in DNA repair and transcriptional regulation. To elucidate the mechanisms by which UBZs recognize ubiquitin, Masato Kawasaki and colleagues solved the crystal structures of the UBZ domains from DNA polymerase (pol) η, Werner helicase‐interacting protein 1 (WRNIP) and Tax1‐binding protein 1 (TAX1BP1). They found that, despite sharing a simple β‐β‐α topology, the ubiquitin‐interaction mode varies among UBZs and can be classified into at least two types: the pol η type and the WRNIP1 type.