A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger domain of WRNIP1

作者：Suzuki Nobuhiro; Rohaim Ahmed; Kato Ryuichi; Dikic Ivan; Wakatsuki Soichi; Kawasaki Masato^*

来源：FEBS Journal, 2016, 283(11): 2004-2017.

DOI：10.1111/febs.13734

• green fluorescent protein
• pol eta
• TAX1BP1
• ubiquitin-binding zinc finger
• WRNIP1

The ubiquitin-binding zinc finger (UBZ) is a type of zinc-coordinating beta-beta-alpha 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) eta 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 eta UBZ, which has been proposed to bind ubiquitin via its C-terminal alpha-helix, ubiquitin binds to a novel surface of WRNIP1 UBZ composed of the first beta-strand and the C-terminal alpha-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 eta type and the WRNIP1 type.

• 出版日期2016-6