Work

Properties of human centrin 2 and cooperative effects between the N- and C-terminal domains

Year: 2025

Type: article

Abstract: -induced HsCen2 aggregation. Interestingly, DNA can bind to HsCen2 or C-HsCen2 or N-HsCen2, and the affinity of C-HsCen2 binding to DNA is stronger than that of intact HsCen2 to DNA. In addition, HsCen2, isolated C-HsCen2, and isolated N-HsCen2 exhibited endonuclease-like activities that induced DNA strand break through the hydrolysis pathway, and the endonuclease-like activity was of the following order: N-HsCen2 > C-HsCen2 > HsCen2. The results are extensively discussed, and the cooperative effect between the N- and C-terminal domains of HsCen2 is explored.

Source: RSC Advances

DOI: 10.1039/d5ra04219d

Authors: Jing Yang, Yaqin Zhao, Binsheng Yang

Institutions: Taiyuan University, Shanxi University

Language: English

Topic: Microtubule and mitosis dynamics

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $1,042

Funders: National Natural Science Foundation of China, Natural Science Foundation of Shanxi Province