Article info Vol. 6  No. 4   pp.  100 ~ 102
Title Purification, crystallization, and preliminary X-ray diffraction data analysis for PB1 dimer of P62/SQSTM1
Authors Ho-Chul Shin1†, Dahwan Lim1,2†, Bonsu Ku1 and Seung Jun Kim1*
Institutions 1Disease Target Structure Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 34141, Republic of Korea, 2Department of Biochemistry, Chungnam National University, Daejeon 34134, Republic of Korea *Correspondence: ksj@kribb.re.kr † These authors contributed equally to this work
Abstract Autophagy is a degradation pathway that targets many cellular components and plays a particularly important role in protein degradation and recycling. This process is very complex and several proteins participate in this process. One of them, P62/SQSTM1, is related to the N-end rule and induces protein degradation through autophagy. The P62/SQSTM1 makes a huge oligomer, and this oligomerization is known to play an important role in its mechanism. This oligomerization takes two steps. First, the PB1 domain of P62/SQSTM1 makes the base oligomer, and then, when the ligand binds to the ZZ domain of P62/SQSTM1, it induces a higher oligomer by the disulfide bond of the two cysteines. To understand the oligomerization mechanism of P62/SQSTM1, we need to know the dimerization of the PB1 domain. In this study, crystals of PB1 dimer were made and the crystals were diffracted by X-ray to collect usable data up to 3.2A. We are analyzing the structure using the molecular replacement (MR) method.