Crystal structures of HpSoj–DNA complexes and the nucleoid-adaptor complex formation in chromosome segregation. Issue 4 (14th December 2018)

• Record Type: Journal Article
• Authors: Chu, Chen-Hsi; Yen, Cheng-Yi; Chen, Bo-Wei; Lin, Min-Guan; Wang, Lyu-Han; Tang, Kai-Zhi; Hsiao, Chwan-Deng; Sun, Yuh-Ju
• Is Part Of: Nucleic acids research. Volume 47:Issue 4(2019)
• Page Start: 2113
• Page End: 2129
• Publication Date: 2018-12-14
• Subjects: Nucleic acids -- Periodicals; Molecular biology -- Periodicals; 572.805
• DOI: 10.1093/nar/gky1251
• Languages: English
• ISSNs: 0305-1048

Abstract

Abstract: ParABS, an important DNA partitioning process in chromosome segregation, includes ParA (an ATPase), ParB (a par S binding protein) and parS (a centromere-like DNA). The homologous proteins of ParA and ParB in Helicobacter pylori are Hp Soj and Hp Spo0J, respectively. We analyzed the ATPase activity of Hp Soj and found that it is enhanced by both DNA and Hp Spo0J. Crystal structures of Hp Soj and its DNA complexes revealed a typical ATPase fold and that it is dimeric. DNA binding by Hp Soj is promoted by ATP. The Hp Soj–ATP–DNA complex non-specifically binds DNA through a continuous basic binding patch formed by lysine residues, with a single DNA-binding site. This complex exhibits a DNA-binding adept state with an active ATP-bound conformation, whereas the Hp Soj–ADP–DNA complex may represent a transient DNA-bound state. Based on structural comparisons, Hp Soj exhibits a similar DNA binding surface to the bacterial ParA superfamily, but the archaeal ParA superfamily exhibits distinct non-specific DNA-binding via two DNA-binding sites. We detected the Hp Spo0J– Hp Soj–DNA complex by electron microscopy and show that this nucleoid-adaptor complex (NAC) is formed through Hp Soj and Hp Spo0J interaction and parS DNA binding. NAC formation is promoted by Hp Soj participation and specific parS DNA facilitation.