Mono-phosphorylation at Ser4 of barrier-to-autointegration factor (Banf1) significantly reduces its DNA binding capability by inducing critical changes in its local conformation and DNA binding surface

Author:

Tang Ming12ORCID,Suraweera Amila1,Nie Xuqiang13,Li Zilin45,Lai Pinglin6,Wells James W.2,O’Byrne Kenneth J.17,Woods Robert J8,Bolderson Emma1,Richard Derek J1

Affiliation:

1. Cancer and Ageing Research Program, Centre for Genomics and Personalised Health, Queensland University of Technology at the Translational Research Institute Australia, Brisbane, Australia

2. Faculty of Medicine, Frazer Institute, The University of Queensland at the Translational Research Institute Australia, Brisbane, Australia

3. College of Pharmacy, Key Lab of the Basic Pharmacology of the Ministry of Education, Zunyi Medical University, Zunyi, China

4. School of Mechanics and Safety Engineering, Zhengzhou University, Zhengzhou 450001, China

5. School of Mechanical, Medical and Process Engineering, Queensland University of Technology, Brisbane, Australia

6. Academy of Orthopedics Guangdong Province, Guangdong Provincial Key Laboratory of Bone and Joint Degeneration Diseases, The Third Affiliated Hospital, Southern Medical University, Guangzhou, China

7. Princess Alexandra Hospital, Brisbane, Australia

8. Complex Carbohydrate Research Centre, University of Georgia, 315 Riverbend Rd, Athens, GA, 30602, USA

Abstract

Mono-phosphorylation of Banf1 inhibits its bending to DNA by inducing steric clashes and unfavourable interactions.

Funder

National Natural Science Foundation of China

China Scholarship Council

Queensland Health

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

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